ID A0A423VWJ8_9PEZI Unreviewed; 829 AA.
AC A0A423VWJ8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RNA-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_08475 {ECO:0000313|EMBL:ROV95468.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV95468.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV95468.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV95468.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROV95468.1}.
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DR EMBL; LKEA01000036; ROV95468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VWJ8; -.
DR STRING; 356882.A0A423VWJ8; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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 Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF3; FI21118P1; 1.
DR PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 112..205
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 220..250
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 306..398
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 627..652
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 725..771
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 93019 MW; 2491B81F4B8B3BB9 CRC64;
MYDDEDRPRY RYRSGSRDYD HGRGANYRRS SRSPRGDREE GEYDYYRSRK DDDDVDDGHA
RRRSPGYHHP HHHSRPQYDA SLSYDDEQAE HHDPDHAPPA RSYAPPPARP SSTIIVEGLP
DDATDDDILD GFASVSPDSK VFHADRVRAI RLRNNKRGRR IGFVEFVDVN AAADFLEYHY
PGLRFQLAHS RGVNSEMISV GINYSWGRED EAVGRDDRSR DMEDWNCPEC AFMNYGSRHQ
CHRCRANRPP AGSLDGHYRA RDDIVSYGPK LTGETDECPQ QIPSQYLVIR GFEPSVTEET
FANGVKKLYV EANPEAKKGT QNKLKSTAPS VRSASLGAKP DSLRRVFLLR DKKTDEVMRY
GFAEFATFED AQAAIEKFKA SPKFTISSKP VSVAFIHNGV FVPHTGRVTD ENSRFVFNPI
YNKDIFLKYW DNRVYPSILS VSGSVDQAKK QSSDNAGSPD KPDEAQDGSG KKLKRFKVGL
PATTAKPAIA MGPQLQMWAK KRAELVGEAQ AQAELAESTA SSSAPSERER GSKRTGVKDS
YLSYSDVDSL SCFLCMRTFA SSQALRDHEV LNKDHIANLS REGKREAATE KLAAEGKRPQ
VVTLRVFDSL HTPAGRMYTS YADRESLHCL ICERKFTKAA VLSLHERESE MHRQNLADQR
NIDRAISQLA RMGKTPRKMM PAKNKGLQYR DRARERRQAY NQPGAPRRKA PKEDTAPVKE
PEKPAPSKGA ALLGKMGWTA GEGLGADRAG RTDVIATDMY AAGVGLGAEG GKIGDAVEEA
ARKTKDNYSD FVEVTRSKAR ERFAHHDASL SIIPILQSGD YRHREEAWF
//
