AIR1_SCHPO
ID AIR1_SCHPO Reviewed; 315 AA.
AC Q9P795;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein air1;
GN Name=air1; ORFNames=SPBP35G2.08c;
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 [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 [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH CID14.
RX PubMed=17512405; DOI=10.1016/j.cell.2007.03.038;
RA Buehler M., Haas W., Gygi S.P., Moazed D.;
RT "RNAi-dependent and -independent RNA turnover mechanisms contribute to
RT heterochromatic gene silencing.";
RL Cell 129:707-721(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-16, 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: Component of the TRAMP (TRF4) and TRAMP5 complexes which have
CC a poly(A) RNA polymerase activity and are involved in a post-
CC transcriptional quality control mechanism limiting inappropriate
CC expression of genetic information. Polyadenylation is required for the
CC degradative activity of the exosome on several of its nuclear RNA
CC substrates like cryptic transcripts generated by RNA polymerase II and
CC III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA
CC processing and degradation intermediates of snRNAs, snoRNAs and mRNAs
CC that accumulate in strains lacking a functional exosome.
CC {ECO:0000269|PubMed:17512405}.
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least mtr4, pap2/trf4 and air1. Component of the TRAMP5
CC complex composed of at least air1, mtr4 and trf5. Interacts with cid14.
CC {ECO:0000269|PubMed:17512405}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AIR1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB87370.2; -; Genomic_DNA.
DR RefSeq; NP_595383.2; NM_001021290.2.
DR AlphaFoldDB; Q9P795; -.
DR BioGRID; 277860; 197.
DR ELM; Q9P795; -.
DR STRING; 4896.SPBP35G2.08c.1; -.
DR iPTMnet; Q9P795; -.
DR MaxQB; Q9P795; -.
DR PaxDb; Q9P795; -.
DR PRIDE; Q9P795; -.
DR EnsemblFungi; SPBP35G2.08c.1; SPBP35G2.08c.1:pep; SPBP35G2.08c.
DR GeneID; 2541349; -.
DR KEGG; spo:SPBP35G2.08c; -.
DR PomBase; SPBP35G2.08c; air1.
DR VEuPathDB; FungiDB:SPBP35G2.08c; -.
DR eggNOG; KOG4400; Eukaryota.
DR HOGENOM; CLU_888910_0_0_1; -.
DR InParanoid; Q9P795; -.
DR OMA; PESTAFC; -.
DR PRO; PR:Q9P795; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0031499; C:TRAMP complex; IDA:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043629; P:ncRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043630; P:ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process; ISO:PomBase.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; ISO:PomBase.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; ISO:PomBase.
DR GO; GO:0016077; P:sno(s)RNA catabolic process; ISO:PomBase.
DR GO; GO:0016076; P:snRNA catabolic process; ISO:PomBase.
DR GO; GO:0016078; P:tRNA catabolic process; ISO:PomBase.
DR InterPro; IPR016713; Air1/2_Saccharomycetales.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 2.
DR PIRSF; PIRSF018162; PolyA_pol_Air1/2; 1.
DR SMART; SM00343; ZnF_C2HC; 5.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..315
FT /note="Protein air1"
FT /id="PRO_0000356248"
FT ZN_FING 89..106
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 127..144
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 189..206
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 315 AA; 35545 MW; 373ECBEF439C3708 CRC64;
MDMTVSNQKA ESDDGSDIDD AALLQKINSL PIDQSITNSV SLEKHDFQGS DDHDSSTDLS
DSTLEDVEGS EWADVSRGRY FGSDPSESIV CHNCKGNGHI SKDCPHVLCT TCGAIDDHIS
VRCPWTKKCM NCGLLGHIAA RCSEPRKRGP RVCRTCHTDT HTSSTCPLIW RYYVEKEHPV
RIDVSEVRKF CYNCASDEHF GDDCTLPSRS NYPESTAFCE ANCPSGNDAS NKEFFETRRK
EFQLERREQN RNQKSSKQRP FHKPGNSLAS RLGSKPKSFK RKHSPPSEEN GNLSFHSSDG
RKFTKTSKKN RKRKW
