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Database: UniProt
Entry: R5IA00_9BACT
LinkDB: R5IA00_9BACT
Original site: R5IA00_9BACT 
ID   R5IA00_9BACT            Unreviewed;       359 AA.
AC   R5IA00;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN   ORFNames=BN796_00800 {ECO:0000313|EMBL:CCY37169.1};
OS   Alistipes sp. CAG:831.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262698 {ECO:0000313|EMBL:CCY37169.1, ECO:0000313|Proteomes:UP000018094};
RN   [1] {ECO:0000313|EMBL:CCY37169.1, ECO:0000313|Proteomes:UP000018094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:831 {ECO:0000313|Proteomes:UP000018094};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC         [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108;
CC         Evidence={ECO:0000256|ARBA:ARBA00034433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108;
CC         Evidence={ECO:0000256|ARBA:ARBA00034429};
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:CCY37169.1}.
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DR   EMBL; CAYB010000139; CCY37169.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5IA00; -.
DR   STRING; 1262698.BN796_00800; -.
DR   Proteomes; UP000018094; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1900723; P:negative regulation of protein adenylylation; IEA:InterPro.
DR   CDD; cd11586; VbhA_like; 1.
DR   Gene3D; 1.10.8.1050; Antitoxin VbhA-like; 1.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   InterPro; IPR033788; VbhA-like.
DR   InterPro; IPR043038; VbhA_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR39560; PROTEIN ADENYLYLTRANSFERASE FIC-RELATED; 1.
DR   PANTHER; PTHR39560:SF1; PROTEIN ADENYLYLTRANSFERASE FIC-RELATED; 1.
DR   Pfam; PF02661; Fic; 1.
DR   Pfam; PF13412; HTH_24; 1.
DR   SUPFAM; SSF140931; Fic-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51459; FIDO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018094};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          100..253
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
SQ   SEQUENCE   359 AA;  41195 MW;  95FDF784A6DEBB40 CRC64;
     MTDFEEYIRQ GEPSRAERAQ AWRTAIGLQD VDGLKPSAYL IDTAREHIEG KITLHDVRQR
     IESYYESRTA RETTDDERTK EADTVSYRIT ELLAEQTFSM SPAELIRIHR YLFTGIYKFA
     GHIRDYNITK KEWVLDGGTI IYAGAGLIMD TLEYDISIER NFSYGGLSAD EAVSHIARFI
     SGLWQIHPFG EGNTRTTAVF LIKYLRNFGF NVENDTFERH SWFFRNALAR ANYNDLKNGI
     TATTEPLERF LRHLILNEKA DLRNRTLHIK ADKNEPLNTD LKVQNGPLNH LAGKVSLVEM
     AVLQLIANNP SIKIEDIATN TKKSRSTIKR AIDRLREKGI IERSGAKKNG SWKILNDRQ
//
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