ID A0A2A2KZB7_9BILA Unreviewed; 144 AA.
AC A0A2A2KZB7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=RRM domain-containing protein {ECO:0000259|PROSITE:PS50102};
GN ORFNames=WR25_16967 {ECO:0000313|EMBL:PAV79346.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV79346.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV79346.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV79346.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC {ECO:0000256|ARBA:ARBA00002001}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H4 family.
CC {ECO:0000256|ARBA:ARBA00006564}.
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:PAV79346.1}.
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DR EMBL; LIAE01007421; PAV79346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2KZB7; -.
DR STRING; 2018661.A0A2A2KZB7; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR047131; RBFOX1-like.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15597; ATAXIN 2-BINDING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR15597:SF44; PIP-1; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 67..143
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 144 AA; 16587 MW; 9E85F91E358D4A93 CRC64;
MFLENVIRDA VTYCEHAKRK TVTAMDVVYA LKRQGRTLVT QLSSNARPAV PISVKPKTKE
PEEFTDNRIY VSNIPFSFRE IDLANMFTPY GRVVNVEIVM NERGSKGFGF VTLDNREGCE
RARRELHGCH VQGRIIEVRM QEEH
//
