ID A0A0A0AM94_CHAVO Unreviewed; 730 AA.
AC A0A0A0AM94;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE Flags: Fragment;
GN ORFNames=N301_10964 {ECO:0000313|EMBL:KGL94135.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL94135.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL94135.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL94135.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; KL871955; KGL94135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AM94; -.
DR STRING; 50402.A0A0A0AM94; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd09033; KH-I_PNPT1; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 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; 1.
DR Gene3D; 1.10.10.400; Polyribonucleotide nucleotidyltransferase, RNA-binding domain; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
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 PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, 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; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
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; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 626..697
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL94135.1"
FT NON_TER 730
FT /evidence="ECO:0000313|EMBL:KGL94135.1"
SQ SEQUENCE 730 AA; 80071 MW; 34073CFEF24250B4 CRC64;
RKMELSSGKL ARFADGSAVV QLGDTAVMVT AVSKTKPSAS QFMPLVVDYR QKAAAAGRIP
TNYLRRELGS TDKEILTSRV IDRSIRPLFP AGYFYDTQIL CNLLAVDGIN DPDVLAINGA
SAALALSDIP WNGPIGAVRV GLVDGETIIN PTRKQMSSSA LNLVVAGAPQ NQVVMLEATA
ENILQQDFCH AIKVGVKHTQ QIIQGIQQLV KEQGVVKRSV QKLFLAPEEI VECAKKLAFN
KIYAVFTDSS HDKISRDEAI NKIRLETEEQ LKEKFPEAEP YEIMESFNVV SKDIFRNLVL
NEYRRCDGRD LTSLRDIKCE VNMFKMLHGS ALFQRGQTQV LCTVTFDSIE SSVKSDLIST
AVSGIKDKNF MLHYEFPPYA TNEIGKVTGM NRRELGHGAL AERALKPIIP QDFPFTIRVT
SEVLESNGSS SMASACGGSL ALMDAGVPVS SAVAGVAVGL ITKCSLEKGD IEDYRLLTDI
LGIEDYYGDM DFKMAGTNKG ITALQVDLKL PGIPIKIVME AIQQATAAKR EILQIMNQTL
AKPRPNRKES GPVVETIHVP LSKRLRFIGP GAYNLKKLQA QTGVTVSQLD EETYSVFAPT
PSAMHEAREF ISEICKDDQE INLEFGAVYT ATITEIRDSG VMVKLYPNMT PVLLHNSQLD
QRKIKHPSAL GLEVGQEIQV KYFGRDPTDG RMRLSRKILQ SPATTVLKTL TDKNSIVLGG
TVPQSSTSSQ
//
