ID K2N1D5_TRYCR Unreviewed; 550 AA.
AC K2N1D5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Polyadenylate-binding protein {ECO:0000256|RuleBase:RU362004};
DE Short=PABP {ECO:0000256|RuleBase:RU362004};
GN ORFNames=MOQ_004370 {ECO:0000313|EMBL:EKF31789.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF31789.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF31789.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF31789.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA.
CC {ECO:0000256|RuleBase:RU362004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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:EKF31789.1}.
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DR EMBL; AHKC01010621; EKF31789.1; -; Genomic_DNA.
DR AlphaFoldDB; K2N1D5; -.
DR SMR; K2N1D5; -.
DR EnsemblProtists; EKF31789; EKF31789; MOQ_004370.
DR OrthoDB; 168698at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR NCBIfam; TIGR01628; PABP-1234; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR PANTHER; PTHR24012:SF695; RRM DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
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; 2.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362004};
KW Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU362004}.
FT DOMAIN 9..86
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 96..173
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 184..265
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 288..367
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 472..549
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
SQ SEQUENCE 550 AA; 61410 MW; 92F37FE9783B5BDE CRC64;
MSNFPAASPS IWVGGLDPNL NEQKLYDHFV RLGPVASVRV CVDSVTQKSL GYGYVNFQNP
ADAEKALDQA GVKLGSKHIR IAKIQRDPSK RRSGVTNIVV KKLPPSVDTY ALKEMFSKYG
RLTAIGLATN ENGESRGYAR ISYEKEESAI QAVQEVNGMV IDDCAITVER YQPHHREEQL
KQFTNLYVKN LDPSVNDEKL KEVFSAFGEV TSAKVRDLGA NQTVGFAYVA YATHEAAAKA
VEELDEKESP LAKEGMKLSV CRFRSRDERQ RERERLRRER QQQHSKYPNL YVKNFDDTVT
SERLKELFER CGETVSVSVM MDRATRVSRC FGFVSFKEQS AASRAIQELH GSTALGPRPL
FVTYALRKDA RRQTLEDMRN KQPRMRQPPM GSLMGGMMGP QLGFMGPQAM FNGVPFVNPR
MSMMPTPMGM GGQLRPMGPT PMNQVRARPM PQRPPMQPIM APPPQPQSLA SQGQNLSTVL
ANLTPEQQKN VLGERLYNHI VAINPAAAAK VTGMLLEMDN GEILNLLDTP GLLDAKVQEA
LEVLNRHMNV
//
