ID A6VU49_MARMS Unreviewed; 365 AA.
AC A6VU49;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Polynucleotide adenylyltransferase region {ECO:0000313|EMBL:ABR69978.1};
GN OrderedLocusNames=Mmwyl1_1047 {ECO:0000313|EMBL:ABR69978.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR69978.1};
RN [1] {ECO:0000313|EMBL:ABR69978.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR69978.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000749; ABR69978.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VU49; -.
DR STRING; 400668.Mmwyl1_1047; -.
DR KEGG; mmw:Mmwyl1_1047; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_1_1_6; -.
DR OrthoDB; 9805698at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:InterPro.
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; IPR012006; CCA_bact.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR PIRSF; PIRSF000813; CCA_bact; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ABR69978.1};
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 7..125
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 153..214
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
SQ SEQUENCE 365 AA; 41454 MW; 56C9C93B879994BD CRC64;
MTNSYQVYLV GGAVRDALLE LPVIDHDWVV TGATPEQLEK KGFQQVGKQF PVFLHPISKE
EYALARKEKK QGEGYTGFIC DFSPEISLEE DLERRDLTIN AIAQDQNGTL IDPFNGQQDL
LDRVFRHVSN AFVEDPLRVL RVARFAARFH HFGFTIAPET MSLMREISSS GELSALSAER
IWKELEKALN TRHANVFFSV LKDANALDKL FPEFIWEDSQ MLTDILNQVG LTPAQRWAIL
CKNTPLTELT QLHQRIRSPN QFKILAEQTR SFLENQHIPM DSTTWENWLI SVNAIKKPQP
FILLIAILSR LTNSKVEDWQ KLRDTIAVIN AASLIKQGFS GAELGQALKK VRTEALDKTL
SPLIS
//
