ID K9EE01_9ACTO Unreviewed; 522 AA.
AC K9EE01;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=tRNA adenylyltransferase {ECO:0000313|EMBL:EKU95429.1};
GN ORFNames=HMPREF9233_00794 {ECO:0000313|EMBL:EKU95429.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95429.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU95429.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
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 -!- 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:EKU95429.1}.
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DR EMBL; AGWL01000003; EKU95429.1; -; Genomic_DNA.
DR AlphaFoldDB; K9EE01; -.
DR STRING; 202789.GCA_001457435_01332; -.
DR PATRIC; fig|883066.3.peg.822; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_6_1_11; -.
DR Proteomes; UP000009888; Unassembled WGS sequence.
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; 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 InterPro; IPR014065; tRNA_adenylyltransferase.
DR NCBIfam; TIGR00277; HDIG; 1.
DR NCBIfam; TIGR02692; tRNA_CCA_actino; 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 SMART; SM00471; HDc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 4: Predicted;
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 ECO:0000313|EMBL:EKU95429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKU95429.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 274..446
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57535 MW; 7B862F37AD23D173 CRC64;
MAISRNSEAA AAAGAGAANL RAKYLLNGQR RLTALPKEIT QLGEIFQRAG HELALVGGPV
RDAFLGLPIH DFDLTTSARP EETEKLLDTW GNTWDIGRDF GTIGAQRAGL TVEVTTYRSD
SYEIGSRKPE VQFGDTLEGD LTRRDFTVNA MAVRLPQLEL VDPCGGLDAL VDGVLETPVT
AAQSFDDDPL RIMRAARFCA QLSFDVAEDV MAAMTDFAPR LEIVSQERIR AELERLIISP
APRRGIELLV YTGVADVVLP EVSGLRGAKD EQGRHKDVYE HTLQVLDNAI ALESVLESTP
SAGGERVAAS EPAPEPEPPV TDEGISPVAR PDFVLRFAAL MHDVGKPATR SFEPDGSVTF
RFHDAVGARM TAKRMKTLRF DKQTTKAVAR LVELHLRAYG FAESGWTDSA VRRFVRDAGP
LLPRLVRLIR ADITSQNRRK VRVLQAANDE LERRIVELHQ REELEAVRPD LDGNDIMEIL
GLAPGPQVGQ AYKYLLGLRL DEGPLGREEA ISRLKQWWEA RA
//
