ID A0A507BSX4_9FUNG Unreviewed; 1153 AA.
AC A0A507BSX4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RRM domain-containing protein {ECO:0000259|PROSITE:PS50102};
GN ORFNames=SmJEL517_g04693 {ECO:0000313|EMBL:TPX32147.1};
OS Synchytrium microbalum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Synchytriales;
OC Synchytriaceae; Synchytrium.
OX NCBI_TaxID=1806994 {ECO:0000313|EMBL:TPX32147.1, ECO:0000313|Proteomes:UP000319731};
RN [1] {ECO:0000313|EMBL:TPX32147.1, ECO:0000313|Proteomes:UP000319731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL517 {ECO:0000313|EMBL:TPX32147.1,
RC ECO:0000313|Proteomes:UP000319731};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
CC -!- SIMILARITY: Belongs to the CAF1 family.
CC {ECO:0000256|ARBA:ARBA00008372}.
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:TPX32147.1}.
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DR EMBL; QEAO01000034; TPX32147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507BSX4; -.
DR STRING; 1806994.A0A507BSX4; -.
DR EnsemblFungi; TPX32147; TPX32147; SmJEL517_g04693.
DR OrthoDB; 276176at2759; -.
DR Proteomes; UP000319731; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR014789; PolyA-riboNase_RNA-binding.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15092; POLY A -SPECIFIC RIBONUCLEASE/TARGET OF EGR1, MEMBER 1; 1.
DR PANTHER; PTHR15092:SF49; POLY(A)-SPECIFIC RIBONUCLEASE PNLDC1; 1.
DR Pfam; PF04857; CAF1; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF08675; RNA_bind; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000319731};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 369..439
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1001..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 128943 MW; 70839363F4698555 CRC64;
MEVLKGSFDA ILPTIAEAIQ QADFVAIDTE LTGLNNGQST AYAALDTPQD RYSKLRKSSQ
QFSITQYGVS CFIWDQKKKS YTSKPFNFYI FPATAKFPFN VFERNWMSQV GSIEFLAKNG
FDFNKWIRHG IPYCSKHEES YIKNQINQVS TQPGIAIDDG NREFVETSLD RVDEWLQNSV
EKSIDIDTQS SYHKKLIGQQ IRQKYNNALG VSLRDRSVQV KRLSDEERDN GVGDQAVQLE
KQLDEIYDTK HICKTIPALA PHFPDSSLEK VYKTTLEPPF EAPTIQIHDD HQRYSTTSAS
YHEAGWDAHA TGAAFARLVA QFQQDTKISP RVSFDEDTLL ECLNRMNMMR SDLAYVHLNG
PDDQPDRSSV LHIFSMPQNY KQKDIEASFD AKEYGSISLQ WINSTSAFIR FESTEKSEKA
LSQHTIASKK ADNLNYGDDM EDGEENAKAT EAPAYHLQRY TDMMAMADGP TAKISNGGEN
GDVSGKRKRP AGVPVFYFGI SAILYIRLKQ FVEKLTGASR ADNPDAKSDW SPWPARYKPF
EGSEYDVVAV IGSNTTWVNV ANPELAKDVA VRKLDFPKPI QWYDILDVYG KNVLTVEGEV
WKYMRRIVAP TFSDRNSGLV HQETIKTCKA MFDAWDKSAA NGSAEVNVSN DSMKLTMFVI
SGAGFGLSLD WNREDQAGYE NHKLSFKQSA GAFLDVSVLF KINAQFDSYL REFIADAKSG
KKMNENNVLR ALVVSTGEDD DFTGKAEASD KRVMTEAEIV GNCFIIMLAG HETTYETPGF
STNETLSNQD IQEELHAEVE RVLGDRDPKY QDYNELKYCQ AVANETLRLF PAVVSIPKWV
PKDGKPQHLG KLVVEPGTHV NIHASALHHD LSYTTQPSDY NADKGLGLLS AFSGPLLAAA
HNELHADKVV LSRSDIGQII AFRADMDSAT RKHATYKFSS SPKAGTVLAF LDMLASQEEF
KGGLVLDSYR QPHEVLCYPD KAASDNDISI MATQSPVLMS GGGSVTIPGT RKRGMTSISE
NSTTTKNSCN SIDITISRSS EKFLSRPIAD VHKVMLLHPS LVLDKPPPAI VSMTLRTTIS
LPPTKWKRMR TQEHLRKDCK DCSIVKKPRE TTAQDYTPAR IWYSAHGGHM NDINKKAIDA
VMLKLFGILE AMK
//
