ID D7L9G2_ARALL Unreviewed; 761 AA.
AC D7L9G2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Polynucleotide adenylyltransferase family protein {ECO:0000313|EMBL:EFH60328.1};
GN ORFNames=ARALYDRAFT_900106 {ECO:0000313|EMBL:EFH60328.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
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DR EMBL; GL348715; EFH60328.1; -; Genomic_DNA.
DR RefSeq; XP_002884069.1; XM_002884023.1.
DR AlphaFoldDB; D7L9G2; -.
DR STRING; 81972.D7L9G2; -.
DR EnsemblPlants; scaffold_304076.1; scaffold_304076.1; scaffold_304076.1.
DR GeneID; 9320135; -.
DR Gramene; scaffold_304076.1; scaffold_304076.1; scaffold_304076.1.
DR KEGG; aly:9320135; -.
DR eggNOG; KOG2159; Eukaryota.
DR HOGENOM; CLU_015786_2_0_1; -.
DR OrthoDB; 5404757at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; IEA:EnsemblPlants.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProt.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:EFH60328.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 92..240
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 268..330
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT REGION 595..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 86183 MW; 2D72556DC4DBF3AA CRC64;
MAGFIRRNGN VFFRSQTLSA FYSKLQRSNC TLAEGVMEKC SSIRSVIDED INSVDTSKWK
KVRASDAGIR NSMIPESSMN VLRLLRRQGF DAYLVGGCVR DLILHRVPKD YDVITTANLK
QIRRLFHRAQ VIGKRFPICH VWMGGSIIEV SSFDTVAHSD SEHEDDLEKS KEKSGVSLDT
EANKNNSLFT MYSGWDVKDC NRWRNSLQRD FTINSLFYNP FELKIYDYAN GMEDLTDLKL
RTLVPAHLSF KEDCARILRG LRIAARLGLS LSKDIETAIP EFVSSVANLD QFRLIMEMNY
MLAYGAAAPS ILLLMKFKLL HVLLPFQAAY LDQASETSLS SSLMLVRLFS NMDKLVSCDQ
PADPKLWIAV LAFHIALVRN PQEAIVVRAF AALLYHRNWS KAVKFAREHE TSVVGYAPEV
SKFSRKRSDE DLAEAVSEFT CLLKDTQYVL TDIEALREAL YLYPDFKFSG LVFIPKRKGR
DVAEGLARLS DVESYESKKE GFSIDYLLLG KGNPCEVRFV LGKIILDTIT EGIVIEPLNS
VKKKQSTSNQ IVSAACLEKK DELFVTKSSK EENNNHTPVY DSNASSVLKI LKRTRKESEQ
KIDQETEVCP RTLSGPAKNQ DQSVVQKLKR RRSKEAQVSE PPKQKTSKRS RSDDQEAVES
ISVPAKNQHQ SNKHDTNAPI CELPKQKTSK NRSKETQKVK HNDLPMKEIQ EAKHGLVSDK
SMSDLLKVLE KSSQQVSSKE KSDSLSSQKT KRPRNLSSLF R
//
