ID S8AHR5_DACHA Unreviewed; 1782 AA.
AC S8AHR5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN ORFNames=H072_3572 {ECO:0000313|EMBL:EPS42394.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42394.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42394.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42394.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is
CC involved in the endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000256|ARBA:ARBA00002863}.
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:EPS42394.1}.
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DR EMBL; AQGS01000114; EPS42394.1; -; Genomic_DNA.
DR RefSeq; XP_011109542.1; XM_011111240.1.
DR STRING; 1284197.S8AHR5; -.
DR eggNOG; KOG1070; Eukaryota.
DR HOGENOM; CLU_000845_0_0_1; -.
DR OMA; GQYLRAY; -.
DR OrthoDB; 167902at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05702; S1_Rrp5_repeat_hs11_sc8; 1.
DR CDD; cd05703; S1_Rrp5_repeat_hs12_sc9; 1.
DR CDD; cd05693; S1_Rrp5_repeat_hs1_sc1; 1.
DR CDD; cd05697; S1_Rrp5_repeat_hs5; 1.
DR CDD; cd05698; S1_Rrp5_repeat_hs6_sc5; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 11.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR048058; Rrp5_S1_rpt_hs11_sc8.
DR InterPro; IPR048059; Rrp5_S1_rpt_hs1_sc1.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR23270; PROGRAMMED CELL DEATH PROTEIN 11 PRE-RRNA PROCESSING PROTEIN RRP5; 1.
DR PANTHER; PTHR23270:SF10; PROTEIN RRP5 HOMOLOG; 1.
DR Pfam; PF00575; S1; 5.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 4.
DR SMART; SM00316; S1; 13.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 11.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50126; S1; 12.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 140..244
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 260..325
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 447..521
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 538..607
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 627..696
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 716..789
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 811..880
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 921..1002
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1035..1106
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1122..1191
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1216..1285
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1303..1374
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1782 AA; 196494 MW; A396ECA8D6831B49 CRC64;
MVNKRKDSPS KGAADTSKST KRQKTTESKE TPASKAAPKP VDAPIQSTLR KSNKEEASFP
RGGASALTPL EYKEVVNEAT REVLFETKDE KDTATEKTPK KRRQPVAKAS SAKKQKKEEA
GDQEPEVKIE PLSYKRLATG QLVFGFISKI TKKDVAIALP NNLVGYAPLT SISEQYTNQL
KASLEDDDMD VDKDEDDESD ETDIPGLDML FEVNQPVRAY VMNVSTGSTS GDKKNRKHIE
LSLLPSLTNP GITQTELVKG TTLQASVKSI EDNGFIMDLG LDFVSGFMGK SDCAAPPNTI
KVGRTFLCHV LGLASGGKVV QLASDFHKSI KGKTGKDASV GDGPTIDCFL PGTLASKVLI
TDVKDNGLVC KLMGSVDVTI DIFHSGCFSS ETLQNKFKAG NNITVRLLAT IPSSEEKKFA
ASLLTHVKEM GPQTHAGKLA LSKLPIGAIK SDAVVKHIIP GVGLILNIGL PATLVFVHIS
RISDKKIDAL LSTGPYKVGS QHAVRLLDYN SMDSLLLGSM EQKVISQRYL RLEDVKPGDV
VKGKITRFTA GGMMVQIEEG MEAYVPEMHM SDVVLQHPEK KFREGAAVKG RILRVDLDLH
RIKMTLKKAI VNSEGPVFAE YIDVEEDEET PGTIVKLMPT GAILEFYGEV KGFLPVSEMS
EAYIKDPQEH FKVGQTLNVH VLTTDPIQKK LRLSCRNNEA ESSKEKAEAL KKIKLGSVVD
GTIVEKSSDD VVVALQEGIK GLIVLGHLGD GSREKNMATF KKLRAGQKLI DLVVLRKDEL
RNIVYLTAKP SLVKAAKSET LIMSFLDVKI GSAVAGFVKD ITHFGIFVSF VGAVTALLPR
KLLPKEVEDL PDFGYQRLQS ITCYVTDINP TKEQFNLSLR PTPVSQPAPA PKPKVQKEQS
DSVSTSVVNP IDSRILTIED FERISATKAR ITAIKPTQLN VDLADNVKGR VDVSEYFNDW
DSIKNKKHAL LRQGLTVGQE IDVKVIGIHD VKSHKYLPIS HRVSGRLPTF ELSAKAQTIK
AKSHHLVTYS ELKKGETYIA FVNNVQDDHL WVNISPSVRG RIKLLEISDD VAALQNLEKR
FPVGAALKVS VLDIDVDAGR LELTARYTGE NKPLDWSNIT EGMMIPAKVS KISEGKVIAQ
LSESLLGSIS LADMADDFDK ADVKNFQKDS IIRVCVLNVD TSNKKIHLST RPSRVLDSSS
KVRDAEVKTA ADIKLSKLYR GFVTNVADNG LYIHLGGAVV ARARIADLSD EYVKDWKKGF
KIHQLVRGKI MSVDLDTNQV SINLKKSVIS GTAKKTMAEY QAGDFVDGHV RKVADFGCFI
VIDGSDNVSG LCHKSQMSSE QEPDPHKLFA EGDLVKAKIL KVDRAKGRIS FGLKASYFED
LPEEELVPKG SEEEQLIIEA SEDEDMEDTD SEEEEEQGGV KLDASSGVTI SGIDRTIAAA
AATKSIWAAD AMDEMFAAPE APSDSESEDE SAKKPKKKNA IKVDLTGELD TRQPQTASDY
ERLLLATPND SLLWMSYMAM TVTNGDTVGA RAIAERALKK IDHRNEDAKL NIWMARLNLE
LEFGTPETFE IAFKSACQYN DSKKIHQGLV SVYIQTGKHE QADETFQSMI KKFSQDEKVW
INYMTYMMEH NRGDEARVML SRALQAIQDV KAHPSLTMKF AQLEYKSGEV EKGRTLFEKL
LAAYPKRLDI WNVYIDLEAK QGDADVIRRL FPRVLKVGKV NAKKANGLFN KWMELEEKFA
PGDKKRREYV MAQAVEFKKK LVEEKEAKAA AGDEDDMEDD DE
//
