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Database: UniProt
Entry: A0A1Y2X4A4_9PEZI
LinkDB: A0A1Y2X4A4_9PEZI
Original site: A0A1Y2X4A4_9PEZI 
ID   A0A1Y2X4A4_9PEZI        Unreviewed;       617 AA.
AC   A0A1Y2X4A4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=K445DRAFT_57877 {ECO:0000313|EMBL:OTB16780.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB16780.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB16780.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB16780.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KZ112934; OTB16780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2X4A4; -.
DR   STRING; 1001832.A0A1Y2X4A4; -.
DR   OrthoDB; 228305at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06133; ERI-1_3'hExo_like; 1.
DR   CDD; cd12452; RRM_ARP_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR   InterPro; IPR047201; ERI-1_3'hExo-like.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR034351; Nrp1_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23111:SF40; RNA-BINDING PROTEIN INVOLVED IN HETEROCHROMATIN ASSEMBLY-RELATED; 1.
DR   PANTHER; PTHR23111; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          253..331
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          352..381
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          429..460
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          556..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  65697 MW;  C34066470A9C7654 CRC64;
     MSSQQTPPPH IDRYVVIHVA TTCDEHGVYV TKDSAEVIEL GWILLDSKSL EEIHRESVLV
     KPINTPITPL CTSLTTLTWE HVRNAGTFRD AVNRFDAFAS EHLTSQNLDF VFVTLDAWDL
     RVQLPREARD KAVVLPPYLQ HSRTFDLRTE YQRWQQHHPE SLPFGPSMLS NICAALEVEP
     VQSSAPIKHN LPFHLQALAP ASPRRAMEEA VTLARVLRGL IRKSQPPQEH PDVLTRPMDA
     RADVRAFLSE RSKVLHMSGL PHDTTQSELE SWFTQFGGRP IAFWTLRTPE QHKPTGTGFA
     VFSSHEEAAE SLCMNGRALN EKAIEVSPSS SRVLDRAAEI LTPFPPSKNR PRPGDWTCPS
     CGFSNFQRRT ACFRCSFPAV SAGPQGDMGY GYGYGPPAMM GPPPHHGGHH GNMGHGGGRM
     GGSGVVPFRA GDWKCGNEVC GYHNFAKNVC CLRCGASRAG AAVVADSGYP SPMDSGSSYG
     MGSGSMAGTP GPGPFASATG PFGASGGYGH HFGGPPSTYA LPSGIGGGAA PYPSLNTHFG
     PAPGAHSAGP FDSRAAEAAF QSASNGPASA GPSNNFYSSQ AENDPFAFLS SGMGGLSVSG
     GDARQNGAGA PSSKSPA
//
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