ID K4IEZ9_PSYTT Unreviewed; 474 AA.
AC K4IEZ9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=tRNA nucleotidyltransferase/CCA-adding enzyme {ECO:0000313|EMBL:AFU67661.1};
GN OrderedLocusNames=P700755_000641 {ECO:0000313|EMBL:AFU67661.1};
OS Psychroflexus torquis (strain ATCC 700755 / ACAM 623).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU67661.1, ECO:0000313|Proteomes:UP000008514};
RN [1] {ECO:0000313|EMBL:AFU67661.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFU67661.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Feng S., Powell S.M., Bowman J.P.;
RT "The complete sequence of Psychroflexus torquis an extreme psychrophile
RT from sea-ice that is stimulated by light.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|RuleBase:RU003953}.
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DR EMBL; CP003879; AFU67661.1; -; Genomic_DNA.
DR RefSeq; WP_015023278.1; NC_018721.1.
DR AlphaFoldDB; K4IEZ9; -.
DR STRING; 313595.P700755_000641; -.
DR KEGG; ptq:P700755_000641; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_1_10; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000008514; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 1.10.246.80; -; 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; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR NCBIfam; TIGR00277; HDIG; 1.
DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR Pfam; PF01966; HD; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 29..157
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 186..245
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 264..346
FT /note="HD"
FT /evidence="ECO:0000259|Pfam:PF01966"
SQ SEQUENCE 474 AA; 54612 MW; 20820196E805AD56 CRC64;
MPDSYYQDAL QHKIFNILSE AADDINVEAY VIGGFVRDFF LKRGKAEDID VVAVGSGIEL
AKKVSEKLPG KPPVKVFKTY GTAMLKIFDL EVEFVGARRE SYTEDSRNPK VEQGTLADDQ
NRRDFTINAL ALQLNKKDFG KLLDPFKGLE DLKTQLIKTP LDPEVTFSDD PLRMIRAIRF
ASQLHFKIDQ KSIQAIKDHS ERIDIVSKER IVTELNKILK SEKPSVGFKL LHDTNLLQRI
LPELTHLEGI DEIDGQKHKD NFWHTLEVVD NISLETNDVW LRWAALLHDI GKAPTKRFHK
KIGWTFHGHE FKGSKMVYQL FKRLKLPLND KMKLVQKLVL LSSRPIAIVD DDVTDSAVRR
LIFDTGDHLD DLMMLCEADI TTKNPKRYKK YHNNFKVVRH RIQEVEERDK VRNFQPPVSG
KEIMETFQIE PCREVGEIKA KIKEAILDGD IPNDYEAAFQ YMLKEGEARG FKQA
//
