ID F1L0M1_ASCSU Unreviewed; 412 AA.
AC F1L0M1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Mortality factor 4-like protein 1 {ECO:0000313|EMBL:ADY43675.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY43675.1};
RN [1] {ECO:0000313|EMBL:ADY43675.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JI169130; ADY43675.1; -; mRNA.
DR AlphaFoldDB; F1L0M1; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.274.30; MRG domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; MORTALITY FACTOR 4-LIKE PROTEIN; 1.
DR PANTHER; PTHR10880:SF48; MRG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS51640; MRG; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 36..80
FT /note="Tudor-knot"
FT /evidence="ECO:0000259|Pfam:PF11717"
FT DOMAIN 187..399
FT /note="MRG"
FT /evidence="ECO:0000259|Pfam:PF05712"
FT REGION 101..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46938 MW; CF32086ABE11E988 CRC64;
MPRKESGGGK EAKDIDKEAV TKSGDATTLA YSLNDKVLCR HLDNLYYEAK IIAVEQTPDG
EPIYTVHYQG WNQRHDEKIR HSVTSERFLE YTPANVERAK AEMRDAQARI QQSKKKGKKS
SGGLDDKRNE GSESRASTPS EKRGASSSRA ASITSDKGAY GTSTAASSAS TSSRKRRSAA
AGSEAERIPD FVRKEEIKIE MPMVLKDILV DDQDMIVRQM YLVRIPARYT VAEIIRQYAD
YTGTSVEARE QLKLEYTDET QLKSMMVTLI ESSLGVQDYF NTALGTQLLY KFERPQYLDL
VNEHTTKKES IKEEQSTKRK RVNDVPTTEE GPAVEETFKP SDFYGFIHLL RLFVRFGSML
SLTSWSDRAL QSIVSHVHNF LKFLEVNRHK FFDIETDYEV ASPEYQRRVW TT
//
