FICD_CAEBR
ID FICD_CAEBR Reviewed; 507 AA.
AC A8X181;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein adenylyltransferase fic-1;
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:Q23544};
DE AltName: Full=De-AMPylase fic-1 {ECO:0000305};
DE EC=3.1.4.- {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q8SWV6};
GN Name=fic-1; ORFNames=CBG05963;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Protein that can both mediate the addition of adenosine 5'-
CC monophosphate (AMP) to specific residues of target proteins
CC (AMPylation), and the removal of the same modification from target
CC proteins (de-AMPylation), depending on the context (By similarity). The
CC side chain of Glu-273 determines which of the two opposing activities
CC (AMPylase or de-AMPylase) will take place (By similarity).
CC Adenylyltransferase that mediates the addition of adenosine 5'-
CC monophosphate (AMP) to specific residues of target proteins. In vivo
CC target proteins include the heat-shock 70 family proteins hsp-1 and
CC hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2.
CC Can AMPylate core histone H3 in vitro (By similarity). Can also act as
CC a phosphodiesterase by mediating removal of ATP (de-AMPylation) from
CC target proteins (By similarity). Decreases susceptibility to
CC P.aeruginosa-mediated killing and might therefore play a role in the
CC innate immune response (By similarity).
CC {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q23544,
CC ECO:0000250|UniProtKB:Q8SWV6}.
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.n1;
CC Evidence={ECO:0000250|UniProtKB:Q9BVA6};
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.n1;
CC Evidence={ECO:0000250|UniProtKB:Q8SWV6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-
CC threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q8SWV6};
CC -!- ACTIVITY REGULATION: The side chain of Glu-273 determines which of the
CC two opposing activities (AMPylase or de-AMPylase) will take place. In
CC response to endoplasmic reticulum stress, mediates de-AMPylase activity
CC (By similarity). Adenylyltransferase activity is inhibited by the
CC inhibitory helix present at the N-terminus: Glu-273 binds ATP and
CC competes with ATP-binding at Arg-414, thereby preventing
CC adenylyltransferase activity (By similarity). In unstressed cells,
CC disengagement of Glu-273 promotes adenylyltransferase activity (By
CC similarity). Activation dissociates ATP-binding from Glu-273, allowing
CC ordered binding of the entire ATP moiety with the alpha-phosphate in an
CC orientation that is productive for accepting an incoming target
CC hydroxyl side chain (By similarity). {ECO:0000250|UniProtKB:A0A061I403,
CC ECO:0000250|UniProtKB:Q9BVA6}.
CC -!- SUBUNIT: Forms homodimers; homodimerization might be required for
CC adenylyltransferase activity. {ECO:0000250|UniProtKB:Q23544}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q23544}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q23544}. Note=Predominantly localized to the
CC endoplasmic reticulum and to the nucleus.
CC {ECO:0000250|UniProtKB:Q23544}.
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC {ECO:0000250|UniProtKB:Q9BVA6}.
CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; HE600909; CAP26391.1; -; Genomic_DNA.
DR RefSeq; XP_002633242.1; XM_002633196.1.
DR AlphaFoldDB; A8X181; -.
DR SMR; A8X181; -.
DR STRING; 6238.CBG05963; -.
DR PRIDE; A8X181; -.
DR EnsemblMetazoa; CBG05963.1; CBG05963.1; WBGene00028317.
DR GeneID; 8575239; -.
DR KEGG; cbr:CBG_05963; -.
DR CTD; 8575239; -.
DR WormBase; CBG05963; CBP01640; WBGene00028317; Cbr-fic-1.
DR eggNOG; KOG3824; Eukaryota.
DR HOGENOM; CLU_040460_0_1_1; -.
DR InParanoid; A8X181; -.
DR OMA; CTEMTLD; -.
DR OrthoDB; 1057856at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR Gene3D; 1.10.3290.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR040198; Fido_containing.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR13504; PTHR13504; 1.
DR Pfam; PF02661; Fic; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51459; FIDO; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endoplasmic reticulum; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..507
FT /note="Protein adenylyltransferase fic-1"
FT /id="PRO_0000381778"
FT TRANSMEM 40..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 146..179
FT /note="TPR 1"
FT REPEAT 180..213
FT /note="TPR 2"
FT DOMAIN 325..460
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT REGION 482..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 269..274
FT /note="Inhibitory (S/T)XXXE(G/N) motif"
FT COMPBIAS 490..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /evidence="ECO:0000250|UniProtKB:A0A061I403"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT BINDING 356..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT BINDING 439..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT SITE 273
FT /note="Important for autoinhibition of adenylyltransferase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA6"
FT MOD_RES 351
FT /note="O-AMP-threonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q23544"
FT MOD_RES 475
FT /note="O-AMP-threonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q23544"
SQ SEQUENCE 507 AA; 56922 MW; 91CAF2A4BD9092EA CRC64;
MSVRRRTHSD DFSFRLERTR RPSKLDVLRE SPTLPVQQGY SLTTVVLVSL VVTLVCQNVA
PPAFSYLNQL IKNSPKRKIP GQSNRLNIGF ISTNSPEKFA PAVQKPTFLV DPIYDEKWKG
VHTAVPVMTT EPEEKRDNNH AKVKEAILAA KAASRSRRDG NLERAVTIME HAMALAPNNP
QILIEMGQIR EMHNELVEAD QCYVKALAYD PGNSEALVLR ARTNPLVSAI DRKMLKTVHD
LRNEFAHLQH STALRRMMRE TYFLYVYHTV AIEGNTLSLG QTRAILESGM VIPGKSIREH
NEVIGMDAAL RFLNCSLLSK EHHEISIDDI LEMHRRVLGN ADPVEAGKIR TTQVYVGKFT
PVAPEYVLEQ LADMVDWLND ESTMAMDPIE RAAIAHYKLV LVHPFTDGNG RTARLLLNLI
MMRSGFPPVI LPVETRAEYY ASLHVANLGD LRPFVRYVAK HSEASIQRYI GAMKTSSGNV
INGEEPNLTA EESKVSEKIE TECRAGS
