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Database: UniProt
Entry: K1Y4W1_MARBU
LinkDB: K1Y4W1_MARBU
Original site: K1Y4W1_MARBU 
ID   K1Y4W1_MARBU            Unreviewed;       634 AA.
AC   K1Y4W1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=RNA binding protein (Arp) {ECO:0000313|EMBL:EKD20144.1};
GN   ORFNames=MBM_02096 {ECO:0000313|EMBL:EKD20144.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20144.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20144.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20144.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH921430; EKD20144.1; -; Genomic_DNA.
DR   RefSeq; XP_007289985.1; XM_007289923.1.
DR   AlphaFoldDB; K1Y4W1; -.
DR   STRING; 1072389.K1Y4W1; -.
DR   GeneID; 18758031; -.
DR   KEGG; mbe:MBM_02096; -.
DR   eggNOG; KOG4198; Eukaryota.
DR   HOGENOM; CLU_022834_2_0_1; -.
DR   InParanoid; K1Y4W1; -.
DR   OMA; NLDRYVV; -.
DR   OrthoDB; 228305at2759; -.
DR   Proteomes; UP000006753; 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; 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; 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:UP000006753};
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          254..332
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          353..382
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          437..468
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          553..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  67037 MW;  BBFF205A48A652BD CRC64;
     MSASAPSQQG NLDRYVVIHV ATTCDEHGVY VTKDSAEVIE LGWILLDAKS CEELHRESVL
     VKPINTPITP LCTSLTTLTW EHVRNAGTFR DAINRFDAFA SEHLTSQSLD FSFVTLDSWD
     LRVQLPREAR DKAVVLPPYL QHSRTFDLRT EYQRWQQHHP ESLPFGPSML SNICAALEVE
     PVQASAPIKH NLPFHLQALA PASPRRAMEE AITLTRVLRG LIRKSQPAHE HPDVLTRPMD
     ARADVRAFLS ERSKVLHMAG LPHDTTQSEL ESWFTQFGGR PIAFWTLRTP DQHKPTGSGF
     AVFSSHEEAA ESLCMNGRAL NEKAIEVSPS SSRVLDRAAE ILTPFPPSKN RPRPGDWTCP
     SCGFSNFQRR TACFRCSFPA MSAGPSGDSM GGYGGGYGYG PPAMMPPPQH MGHHGGMGGG
     HGGGGRMGGG GGVVPFRAGD WKCGSEGCGY HNFAKNVSCL RCGASRAGAA VVADSGYPSP
     MDTPSNYGGM GPGSMAGTPG PGPFTSAAGG GFSSGGGYGN QHYGGPQSTY ALPSGLGAST
     GPYPGSLNTH FSSAGASSHS AGPFDSRAAE AAFQSASNGP ASAGPGNNFY SSQSESDPFA
     FLSTGMSNMS MGSGDARQNS GSANLPPSKS PGAQ
//
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