LAH1_SCHPO
ID LAH1_SCHPO Reviewed; 298 AA.
AC P87058; O13362; Q10458;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=La protein homolog;
DE AltName: Full=La autoantigen homolog;
DE AltName: Full=La ribonucleoprotein;
GN Name=sla1; Synonyms=lah1; ORFNames=SPAC57A10.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9404894;
RA van Horn D.J., Yoo C.J., Xue D., Shi H., Wolin S.L.;
RT "The La protein in Schizosaccharomyces pombe: a conserved yet dispensable
RT phosphoprotein that functions in tRNA maturation.";
RL RNA 3:1434-1443(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Utsumi R.R.U.;
RT "Screening of S. pombe cDNA library using E. coli defective in signal
RT transduction: cloning and DNA sequence of La-like protein (SLA1).";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-124, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Binds to the precursors of polymerase III RNAs. Functions in
CC tRNA maturation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF022949; AAB82145.1; -; mRNA.
DR EMBL; AB011371; BAA24981.1; -; mRNA.
DR EMBL; CU329670; CAB08173.1; -; Genomic_DNA.
DR PIR; T38937; T38937.
DR PIR; T43542; T43542.
DR RefSeq; NP_593315.1; NM_001018746.2.
DR AlphaFoldDB; P87058; -.
DR SMR; P87058; -.
DR BioGRID; 278030; 38.
DR STRING; 4896.SPAC57A10.10c.1; -.
DR iPTMnet; P87058; -.
DR MaxQB; P87058; -.
DR PaxDb; P87058; -.
DR PRIDE; P87058; -.
DR EnsemblFungi; SPAC57A10.10c.1; SPAC57A10.10c.1:pep; SPAC57A10.10c.
DR GeneID; 2541530; -.
DR KEGG; spo:SPAC57A10.10c; -.
DR PomBase; SPAC57A10.10c; sla1.
DR VEuPathDB; FungiDB:SPAC57A10.10c; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_043291_1_0_1; -.
DR OMA; KFLWKIY; -.
DR PhylomeDB; P87058; -.
DR PRO; PR:P87058; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:PomBase.
DR GO; GO:0000049; F:tRNA binding; IDA:PomBase.
DR GO; GO:0042780; P:tRNA 3'-end processing; IMP:CAFA.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IMP:CAFA.
DR GO; GO:0061818; P:tRNA folding; IMP:PomBase.
DR GO; GO:0008033; P:tRNA processing; IMP:CAFA.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..298
FT /note="La protein homolog"
FT /id="PRO_0000207607"
FT DOMAIN 57..148
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 154..236
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 188
FT /note="M -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 34616 MW; 64E6AB99940B87F4 CRC64;
MSTEEQKEEI KDISSKQENS SEVPKAEEAG KVVESQKDTT SEEKKEETTE KKEDDGKKDL
SFDEAEVLKQ VEFYFSDTNL PHDKFLWTTS QKNDGWVPIQ TIANFKRMRR FQPLEAIVNA
LRKSPELLEV DEAGEKVRRM IPLVRVDNKS VMERSVYCKG FGDEKDDTQI ALEKFFEENA
GPISAVRMRR DDDKKFKGSV FVEFKEPDVA NKFLEKVKTA PLKWGEDELT IMSKKEYVDM
KAELHKNDPP KFSSKRRRFD AFKEMDRQRP GKYSNRGRKF KKQRSSNASE EKPSAASE
