ID A0A1Y2DV20_9PEZI Unreviewed; 775 AA.
AC A0A1Y2DV20;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Polyadenylate-binding protein {ECO:0000256|RuleBase:RU362004};
DE Short=PABP {ECO:0000256|RuleBase:RU362004};
GN ORFNames=BCR38DRAFT_345745 {ECO:0000313|EMBL:ORY62495.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62495.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY62495.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62495.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY62495.1}.
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DR EMBL; MCFJ01000009; ORY62495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DV20; -.
DR STRING; 1141098.A0A1Y2DV20; -.
DR InParanoid; A0A1Y2DV20; -.
DR OrthoDB; 21912at2759; -.
DR Proteomes; UP000193689; 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 CDD; cd12381; RRM4_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; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU362004};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
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}.
FT DOMAIN 64..142
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 152..229
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 245..322
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 348..466
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 679..756
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 317..344
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 383..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 83489 MW; 238B426049D8B7B2 CRC64;
MAAATTSGAV DQLAADLGNA SLNGGDVKTP AINTNVASDA QGDDLDTAGP TPSSAQTPHP
QASASLYVGE LDPSVTEAML FELFSQIGSV ASIRVCRDAV TRRSLGYAYV NYNTTSDGER
ALEELNYTQI KGRPCRIMWS QRDPNLRKSG QGNIFIKNLD AAIDNKALHD TFAAFGNILS
CKVAQDENGN SKGYGFVHYE TDEAAAAAIK HVNGMLLNEK KVYVGHHIPK KDRQSKFEEM
KANFTNVYVK NINPEASDDD FRLLFEAFGD VTSSSLARDQ EGKSRGFGFV NFTTHEAAAK
AVDDLNGKDF QGQDLYVGRA QKKHEREEEL RKSYEAARQE KANKYQGVNL YIKNLNDDVD
DDKLRVLFSE FGPITSAKVM RDSLSESGDD EKDKENQKET IDEVKEEEGE KEEGEKKEKK
GDRKLGKSKG FGFVCFANAD DATKAVAEMN QRMIEGKPLY VALAQRKDVR KSQLEASIQA
RNTLRMQQAA AAAGMPQQFM QPPVYYAPGQ PFPPGGRSGI PFPQPGMGMP GVQGVRPGQF
PNYGAPQGGR GAPVPQQLPP QMYMPGQFPP GAPFGNPSGN PQYMAAMAQA QQAALGGGRG
GPAGRGPMQG MPNMPAMPGV GGPGMPGYPP NARQGSGAAG RGGMNARNGQ MGQFPQGGRG
MPNQQMGAPI PGQDLTTGSL LQSQLQSVAG NPQQQKQMLG EVIFPKIQAL QPELAGKITG
MLLEMDNAEL VNLIEDESAL RAKVDEAMAV YDEYVKTQGG EAEGEKKEEK PEEKA
//
