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
//