ID M2QRJ2_CERS8 Unreviewed; 1277 AA. AC M2QRJ2; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 10-FEB-2021, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMD34805.1}; GN ORFNames=CERSUDRAFT_116989 {ECO:0000313|EMBL:EMD34805.1}; OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia OS subvermispora). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Polyporales; Gelatoporiaceae; Gelatoporia. OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34805.1, ECO:0000313|Proteomes:UP000016930}; RN [1] {ECO:0000313|EMBL:EMD34805.1, ECO:0000313|Proteomes:UP000016930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:EMD34805.1, RC ECO:0000313|Proteomes:UP000016930}; RX PubMed=22434909; DOI=10.1073/pnas.1119912109; RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D., RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D., RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T., RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J., RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K., RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A., RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M., RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K., RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A., RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D., RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J., RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P., RA Martinez A.T., Vicuna R., Cullen D.; RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete RT chrysosporium provide insight into selective ligninolysis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012). CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body CC {ECO:0000256|ARBA:ARBA00004201}. 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; KB445802; EMD34805.1; -; Genomic_DNA. DR EnsemblFungi; EMD34805; EMD34805; CERSUDRAFT_116989. DR HOGENOM; CLU_004235_2_0_1; -. DR OrthoDB; 562895at2759; -. DR Proteomes; UP000016930; Unassembled WGS sequence. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro. DR Gene3D; 3.30.40.10; -; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR031127; E3_UB_ligase_RBR. DR InterPro; IPR002867; IBR_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR044066; TRIAD_supradom. DR InterPro; IPR027370; Znf-RING_LisH. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR000571; Znf_CCCH. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR11685; PTHR11685; 1. DR Pfam; PF01485; IBR; 2. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR SMART; SM00647; IBR; 2. DR SMART; SM00184; RING; 1. DR SMART; SM00360; RRM; 1. DR SMART; SM00356; ZnF_C3H1; 3. DR SUPFAM; SSF54928; SSF54928; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS51873; TRIAD; 1. DR PROSITE; PS50103; ZF_C3H1; 3. DR PROSITE; PS50089; ZF_RING_2; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 4: Predicted; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000016930}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00723}. FT DOMAIN 31..58 FT /note="C3H1-type" FT /evidence="ECO:0000259|PROSITE:PS50103" FT DOMAIN 137..164 FT /note="C3H1-type" FT /evidence="ECO:0000259|PROSITE:PS50103" FT DOMAIN 216..242 FT /note="C3H1-type" FT /evidence="ECO:0000259|PROSITE:PS50103" FT DOMAIN 592..679 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT DOMAIN 1069..1277 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS51873" FT DOMAIN 1073..1114 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 1249..1274 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT ZN_FING 31..58 FT /note="C3H1-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723" FT ZN_FING 137..164 FT /note="C3H1-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723" FT ZN_FING 216..242 FT /note="C3H1-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 255..277 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 285..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 16..30 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..345 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 362..390 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..460 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1277 AA; 142335 MW; 3B271611970E66FF CRC64; MAVTPHSSVA ATRPTVESHD HSDKTRQEIK PAEREVCRNF LRGRCNWGSR CLRFHPESRD VVASNYNKPR PGEASSPFVP PQVESRQRPA QPIYTDRFNR VHCAPQSQPA VQPLPGRPTS VTNAGQQAFV DDARQARKSD EICDNYQKGR CQWGGKCHRK HVYSEVGNVS SAPSDRIIPT QGKQGFERPL PPEADYAALS TILTPPERTA VLRTTPIPPQ ICRDFVRGRC TRNECRRRHP PPDVCAKYII NGNHATEPRA PDATVPSSPI DAERSMPSLT WSTSTIASTT HPRTPPHSKD ATINHDKELW DMLSIHRESP RDESPEAPTV KLPASKNSSI EQPTGKGKAK ASVNDIKSVQ ESPHSKPSKD DKGKARAVDR SAREKKQSHN GAPTHNLIRL QDVPKPTEQP KVEAGTSKQT DQKDEQRVGG AQRRSRRRGR SEQQVKVDES DNENVKTRGS VEKQVVDPPH ASASSSSTSG IPAFEARTAQ PIDRLGGQIP LAQRPVPAAP QYIPGQNGIP LVPPGLGLEH KIAEAARMAE AARMAEAARM AEASSSRKTQ PETFAITVLD STKVTFGPGF EVRQVVTGFE SREIVIDHLP WDVTVNELSE ELQMFGEVVA VHLPERVKPK NKRKHKTKEY PDVSARVTFS SHEEAAEAAV ELDGATFSDR PVSVHLSSTK STSYGKGFLR EGDVVVELPV ASRIAYAGYK TQEEADRVIA IANCSEYRGC WITAARYVGL PSVGMYNVKF WGMPTDLKRG DLEVYGPYQG MAVEAPKYES TERALRCLRR LLEGFGELQS FEVPQGPYKN GVVRVRAHFA SAQVADHFCR KNSGRAQRWL GEQQMWAKHI RTILYTLPPD VFDVLAPEIM LLRSFFQEQS RNTSIDVRDK RTNVMPTAPV SVKLGARDGM QTLTRLKTSF ENLLRGEKLT RHGAIVWDEY FGRRAGSLYL EDLQKSHPGT MINRDPLRRT IALFGPAEKR EVLRDAILAK VTSLRSAKVY TLRLPPTMVG IFMSADLLKL QQELGHENIW VDLTNRLLKV RGSDDAYKVA QLAVLHATQE PRPRSAKPRS GACPVCLSEV TMPVTLTCGH SWCKACISRY IVSVIDTKLF PLTCLGEGGK CSHRLPLRIA QELISPSDFD ALTHAALLAH VHSHPKEFHY CPAPDCTQIY RTAPRNANLQ CPSCFTRICP KCNLEFHENR RCQADIDEDQ KLFEDWKATH DVKNCPGCDA PIERNAGCNH MMCIRCTTHI CWFCEKTFKR SDEVYDHMHS VHGGIGV //