ID A0A1V6PDC1_PENDC Unreviewed; 743 AA.
AC A0A1V6PDC1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Polyadenylate-binding protein {ECO:0000256|RuleBase:RU362004};
DE Short=PABP {ECO:0000256|RuleBase:RU362004};
GN ORFNames=PENDEC_c008G06419 {ECO:0000313|EMBL:OQD75080.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD75080.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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.
CC {ECO:0000256|ARBA:ARBA00024761}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362004}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000256|ARBA:ARBA00008557, ECO:0000256|RuleBase:RU362004}.
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:OQD75080.1}.
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DR EMBL; MDYL01000008; OQD75080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PDC1; -.
DR STRING; 69771.A0A1V6PDC1; -.
DR OMA; QQPGFMP; -.
DR OrthoDB; 21912at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12378; RRM1_I_PABPs; 1.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12380; RRM3_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
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; IPR034364; PABP_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012:SF491; POLYADENYLATE-BINDING PROTEIN; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
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; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362004};
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU362004};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transport {ECO:0000256|ARBA:ARBA00022816}.
FT DOMAIN 48..126
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 136..213
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 229..306
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 332..465
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 637..714
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 80519 MW; 8E55F7BF6A89DC15 CRC64;
MSAETATNPP VAEAAANGSP EANGTPAPAA APETSGEGAA ANNQPHSASL YVGELDPSVT
EAMLYELFSS IGQVASIRVC RDAVTRRSLG YAYVNYNNTA DGERALEDLN YTLIKGKPCR
IMWSQRDPAL RKTGQGNVFI KNLDNAIDNK ALHDTFAAFG NILSCKVAQD EFGNSKGYGF
VHYETAEAAN QAIKHVNGML LNDKKVFVGH HISKKDRQSK FEEMKANYTN IYVKNLELEI
SDDEFRTMFE AFGEITSATL SHDQEGKSRG FGFVNYSTHE SAQAAVEEMN DKEVKGQKLY
VGRAQKKHER EEELRKQYEA ARVEKASKYQ GVNLYVKNLT DDVDDDKLRD LFTPYGTITS
AKVMRDTVSE RSPTPEADEK DKENKAESKE EGEKAETAED KPEGEKKEED GEEQEGEKSE
KKTLGKSKGF GFVCFSSPDE ASKAVTEMNQ RMVNGKPLYV ALAQRKDVRR SQLEASIQAR
NTIRQQQAAA AAGMPQPYMQ PAVFYGPGQQ GFIPAGQRGM AFPPQAGMVM PGMPGRPGQF
PGPFPQQGGR GMGPNQQMPP NFQGMPMAMQ GPGMPNGMGY PMQVPAFGRG AGGRGQVPGM
PMGQGMRGGP GYGRGGPQMG RGQGRGQAPA GQPGRDEPAS SNPALVAAPP AQQKQMLGEA
LYPKIQAQQP ELAGKITGML LEMDNAELLG LLDDEEALRA KVDEALSVYD EYMKNKDNTE
GEAAGEAKPE EAAKEASSEE NKS
//
