ID A0A1Y1IEP9_KLENI Unreviewed; 944 AA.
AC A0A1Y1IEP9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE AltName: Full=Polynucleotide phosphorylase 1 {ECO:0000256|ARBA:ARBA00031451};
GN ORFNames=KFL_005190070 {ECO:0000313|EMBL:GAQ89415.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ89415.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ89415.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ89415.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; DF237468; GAQ89415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1IEP9; -.
DR STRING; 105231.A0A1Y1IEP9; -.
DR OMA; IQLDCKP; -.
DR OrthoDB; 437922at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR FunFam; 3.30.230.70:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 2.40.50.140:FF:000189; Polyribonucleotide nucleotidyltransferase, putative; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01595; PNPase; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR NCBIfam; NF008805; PRK11824.1; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF16; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
DR Pfam; PF00575; S1; 2.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAQ89415.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 716..786
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 851..920
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 793..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..822
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 102390 MW; 99B42696669D394B CRC64;
MASAQARRRC LALVAHVWGR PGAVAEAGRL SHGARQSHKA LSGSLRRDPF TDGLGQFHTR
GFASVSAQPT GEPEAAETPV GRQYPAVGQS FKETAPIEGG SLTLETGKLA RLADAAVVVG
FNETKVLCTA IASRRMDSAQ SFLPLTVDYR EKDYAQGKIP GGYFRREGAP QTRELLCSRL
IDRAMRPLFP EGFYCETQLL ANVLSLDGSQ DPDVLAINGA SAALTISDIP WNGPVGAVRI
ARINGRLVVN PGLEDWGKTD LSLVYAGTER DCVMMDVQAK EISNEDLAQA LRLAHQEAQK
VLDVQRRLAQ QVNHAKRERM LEEISEELVE RIREAAGAKI SAIMEDPSYG KQERGKALAE
VEQEVRAQFE EAGDADAVQK LPLAFDELKW RIIRRNIIDR GVRPDHRPLD QVRPIHCEAD
FLPALHGSSL FSRGNTQVVC TVTLGSVLDA QKLDTMGGPD SKRFMLHYSF PPYATNEVKR
VGAVNRREVG HGMLAEKALA AVMPDDDAFP FTVRVTSECT ASDGSSSMAT VCGGSLALMD
AGVPITKHVA GVSVGLFTDT DADNTVRNYK LVTDIVGLED HLGDMDFKVA GTRDGVTAIQ
LDMKLPGIPL EILVEGLDAA QDARRKVITL MEQEIAKPRE VPKDSHPRLA TLPVDRASLG
KVIGPLGATI KGIQAESGAR LKVEDGGVQI FAKDTASFNL ARHLIEMAVG KDVEIGKVYD
GVVTSVRDYG ALVELDGTGG QEGLLHISEI SENKIKRVED VMREGDRVRV LCTGRNIRGD
TRLSIKALNR ADSAGSSDSE DYSPGSDSDA SSSYRSSSFR GDGPSGAERG EGGTPRREPT
RRITEDNVEL GKTYRAKVVS VRDYGAFLEL ETGEQGLLHV SQISHGFITS IKDHVTLDQE
LEVVVVKEPR DGNGVTFSRL PLLRKPPKRT TNSPIVIPGR RNES
//
