ID   PABP_NEOFI              Reviewed;         751 AA.
AC   A1D4K4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
DE            Short=PABP;
DE            Short=Poly(A)-binding protein;
DE   AltName: Full=Polyadenylate tail-binding protein;
GN   Name=pab1; ORFNames=NFIA_020550;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important
CC       mediator of the multiple roles of the poly(A) tail in mRNA biogenesis,
CC       stability and translation. In the nucleus, involved in both mRNA
CC       cleavage and polyadenylation. Is also required for efficient mRNA
CC       export to the cytoplasm. Acts in concert with a poly(A)-specific
CC       nuclease (PAN) to affect poly(A) tail shortening, which may occur
CC       concomitantly with either nucleocytoplasmic mRNA transport or
CC       translational initiation. In the cytoplasm, stimulates translation
CC       initiation and regulates mRNA decay through translation termination-
CC       coupled poly(A) shortening, probably mediated by PAN (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC       {ECO:0000305}.
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DR   EMBL; DS027688; EAW23347.1; -; Genomic_DNA.
DR   RefSeq; XP_001265244.1; XM_001265243.1.
DR   AlphaFoldDB; A1D4K4; -.
DR   SMR; A1D4K4; -.
DR   STRING; 36630.CADNFIAP00001661; -.
DR   EnsemblFungi; EAW23347; EAW23347; NFIA_020550.
DR   GeneID; 4591237; -.
DR   KEGG; nfi:NFIA_020550; -.
DR   VEuPathDB; FungiDB:NFIA_020550; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   OMA; ASPMEQK; -.
DR   OrthoDB; 1027234at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd12379; RRM2_I_PABPs; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR036053; PABP-dom.
DR   InterPro; IPR006515; PABP_1234.
DR   InterPro; IPR002004; PABP_HYD.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR045305; RRM2_I_PABPs.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 4.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   SUPFAM; SSF63570; SSF63570; 1.
DR   TIGRFAMs; TIGR01628; PABP-1234; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..751
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295395"
FT   DOMAIN          52..130
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          140..217
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          233..310
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          336..458
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          646..723
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  81197 MW;  810F298DD5B53CB7 CRC64;
     MSAEVSTTPA ADNTVNGTPE ATNPAATSAP EVTAVESASP SATPSANQPH SASLYVGELD
     PSVTEAMLYE LFSSIGQVAS IRVCRDAVTR RSLGYAYVNY NNTADGERAL EDLNYTLIKG
     KPCRIMWSQR DPALRKTGQG NVFIKNLDAA IDNKALHDTF AAFGNILSCK VAQDEFGNSK
     GYGFVHYETA EAANNAIKHV NGMLLNDKKV FVGHHISKKD RQSKFEEMKA NFTNVYIKNI
     DQEVTDEEFR KMFEKFGEIT SATLSRDQEG KSRGFGFVNF STHDSAQAAV DEMNDKEIKG
     QKLYVGRAQK KHEREEELRK QYEAARLEKA SKYQGVNLYV KNLTDDVDDE KLRELFSPFG
     TITSAKVMRD TVTAGETSES EKEKESNKEN EKEGEEKTEE KPKESEEEAK KTEKKILGKS
     KGFGFVCFSS PDEASKAVTE MNQRMVNGKP LYVALAQRKD VRRSQLEASI QARNTIRQQQ
     AAAAAGMPQP YMQPAVFYGP GQQGFIPAGQ RGGMPFAPQP GMVMGIPGGR PGQYPGPFPG
     QQGGRGMGPN QQIPPNFQGI PMGAMQGPGG IPNGMGYPQM AQVQFGRGAG GRGQVPGMPM
     GQGMRGPGYG QGRGGAPVQG GPRPQGGRGQ PAAAPPAAGR EEVPATGGLT AQTLNAVPPP
     QQKQMLGEAL YPKIQAQQPE LAGKITGMLL EMDNTELLGL LEDEEALRAK VDEALSVYDE
     YMKNKGEGEA PAEPAKPKED AAETATEENK S