ID A0A0F4GKX7_9PEZI Unreviewed; 730 AA.
AC A0A0F4GKX7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Rna binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TI39_contig440g00001 {ECO:0000313|EMBL:KJX98064.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX98064.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX98064.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX98064.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJX98064.1}.
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DR EMBL; LAFY01000432; KJX98064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GKX7; -.
DR STRING; 1047168.A0A0F4GKX7; -.
DR OrthoDB; 228305at2759; -.
DR Proteomes; UP000033647; 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:UP000033647};
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 324..402
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 431..460
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 521..552
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 76663 MW; 33F2EDE258FE7EAD CRC64;
MATPTQPQQY GGGNPHPTPA SQSGAPSGQQ QQQQQQSAYP SERTASSAPV PYQQQNQQSQ
QQQQQGPAQA QFEKYCIIHI ATTCDEHGVY VTKDSAEVIE IGWVVVDAQN PERELHRESV
LVRPVNTPIT PLCTSLTTLT WEHVKNAGTF RDAINTFDAY ASENLVPKDA GPGANPTFAF
VTLTPWDLRV QLPREARDKN VVLPPYLQHP VLFGLRGEYQ LFQSHHPETL AFSSTSLSSI
CAGLEVEEVR SSGKVTGGLP FHLQALAPSS PRRALEEALT LTRCLNSLVT KSRPSNTSSG
TPDVLQRPID ARSDVRAFLG ERSKVLHLSG LPHDTTQSEL ESWFTQFGGR PIAFWTLRTP
EGGKPSGSGF VVFGSHEEAA ESLSMNGRAL NDRAIEVAPS SARVLDRAAH SQPPGGPPLL
TPFPPSKNRP RPGDWTCPSC GFSNFQRRTA CFRCSFPAMG ASGPDPYSQP YGGMQPPAYG
GGNYGHPGMM QGHMHGGNQY GGGMGGMGGG SSGRGGIVPF RAGDWKCGNE GCGYHNFAKN
VSCLRCGASR SNAAVVAESG MTSFPGNSYG PPPNMPMQSM DSSSYGGMQQ PSGGYGGSGM
GGPPGGFGGQ SFGPPSTYAL PSGIAAPSPY GPYSQMSGPP GGMHSQQGGF DSRAEQAFNN
HGSHGPQQGG PPGGYLNGGY GNTGGYGGGP GGNDGSADPF SFLSSGMGQL GINDGGDNRR
NGQGGAKSPQ
//
