ID A0A163JNY1_DIDRA Unreviewed; 749 AA.
AC A0A163JNY1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=GTP binding {ECO:0000313|EMBL:KZM26482.1};
GN ORFNames=ST47_g2363 {ECO:0000313|EMBL:KZM26482.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM26482.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM26482.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM26482.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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:KZM26482.1}.
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DR EMBL; JYNV01000103; KZM26482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JNY1; -.
DR STRING; 5454.A0A163JNY1; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd05791; S1_CSL4; 1.
DR CDD; cd04128; Spg1; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR039771; Csl4.
DR InterPro; IPR019495; EXOSC1_C.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR017231; Small_GTPase_Tem1/Spg1.
DR PANTHER; PTHR12686; 3'-5' EXORIBONUCLEASE CSL4-RELATED; 1.
DR PANTHER; PTHR12686:SF8; EXOSOME COMPLEX COMPONENT CSL4; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF10447; EXOSC1; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF110324; Ribosomal L27 protein-like; 1.
DR PROSITE; PS51419; RAB; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 549..584
FT /note="Exosome complex component N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14382"
FT DOMAIN 658..696
FT /note="Exosome complex component CSL4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10447"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 81606 MW; B5BC8689428728C4 CRC64;
MDAPPEQQQP VADAQDAQKH AEHTLDVDAD ASSSTVTANP VSPPPHFHPS NASSNGYTPD
PPRPSTSYSD TGYQYPHHGA RFNSSDADTP PRHPYHDGTK ETHMAHPHSR PSSQMGRYST
SDAGARSNSY QDQNARGAQP AQEPAKNSSV VIKVGMVGDA QIGKTSLMVK YVEGSWDEDY
IQTLGTYSAP CILHHPHSLT TYTGVNFMEK TISIRNTEIT FSIWDLGGQR EFVNMLPLVC
NDAVAILFMF DLTRKSTLNS IKEWYRQGRG FNKTAIPFLV GTKYDHFVNF PREEQEEISN
QAKRFARAMK ASLIFSSTSH SINVQKADLQ DCPVQGIRPQ VHHPGDRKRR RASPPLPGRL
AAAAAAAAAF FSERMILMIF LRGIAYLGDW SNVPRAECWF YKMALVWLGL HIRFAATGLE
PFTIRSVESS LYRTAPRVAA AFVPAPAHGS PSLGPLATTY CSVLSKFGNP ADPRIGESAA
TKSSDLAASP PTPTLDTDTN TSTNTNIHRQ PQDGYQPSSK TSIPVQNCNS RACHVDAATY
STAMAVPPVA LPGQLLGSAD KYLPGPGTHM HDSQIYASIA GPVITSATPK TTQTKPSPLL
SIQRPSTSTD PGILGTGSGG GGTILPEVNS IVLALITRLG PRFATCEILV IDNVVCRESF
QGQIRREDIR ATEKDKIKME ESFRVGDLIR GTVISLGDQS NYYVSTSENE FGVVMARSEE
GRLMYPVSWK EFRDPVTGRG ESRKAAKPF
//
