FICD_DANRE
ID FICD_DANRE Reviewed; 449 AA.
AC Q6ZM51;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein adenylyltransferase FICD;
DE EC=2.7.7.n1;
DE AltName: Full=AMPylator FICD;
DE AltName: Full=FIC domain-containing protein;
GN Name=ficd; ORFNames=si:ch211-191d15.5, zgc:110336;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adenylyltransferase that mediates the addition of adenosine
CC 5'-monophosphate (AMP) to specific residues of target proteins.
CC {ECO:0000250}.
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 -!- 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 -!- ACTIVITY REGULATION: Adenylyltransferase activity is inhibited by the
CC inhibitory helix present at the N-terminus: Glu-224 binds ATP and
CC competes with ATP-binding at Arg-364, thereby preventing
CC adenylyltransferase activity. Activation dissociates ATP-binding from
CC Glu-224, allowing ordered binding of the entire ATP moiety with the
CC alpha-phosphate in an orientation that is productive for accepting an
CC incoming target hydroxyl side chain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}.
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DR EMBL; AL845326; CAE50173.1; -; Genomic_DNA.
DR EMBL; BC092885; AAH92885.1; -; mRNA.
DR RefSeq; NP_001017794.1; NM_001017794.2.
DR RefSeq; XP_005165169.1; XM_005165112.3.
DR AlphaFoldDB; Q6ZM51; -.
DR SMR; Q6ZM51; -.
DR STRING; 7955.ENSDARP00000123219; -.
DR PaxDb; Q6ZM51; -.
DR Ensembl; ENSDART00000144232; ENSDARP00000123219; ENSDARG00000035595.
DR Ensembl; ENSDART00000183051; ENSDARP00000145045; ENSDARG00000035595.
DR GeneID; 334648; -.
DR KEGG; dre:334648; -.
DR CTD; 11153; -.
DR ZFIN; ZDB-GENE-030131-6588; ficd.
DR eggNOG; KOG3824; Eukaryota.
DR GeneTree; ENSGT00390000008873; -.
DR HOGENOM; CLU_040460_0_0_1; -.
DR InParanoid; Q6ZM51; -.
DR OMA; CTEMTLD; -.
DR OrthoDB; 1057856at2759; -.
DR PhylomeDB; Q6ZM51; -.
DR TreeFam; TF314692; -.
DR PRO; PR:Q6ZM51; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035595; Expressed in ovary and 27 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Repeat; TPR repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..449
FT /note="Protein adenylyltransferase FICD"
FT /id="PRO_0000317304"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 96..129
FT /note="TPR 1"
FT REPEAT 130..163
FT /note="TPR 2"
FT DOMAIN 275..410
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT MOTIF 220..225
FT /note="Inhibitory (S/T)XXXE(G/N) motif"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 250..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 358..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 50204 MW; 36B7667AAB8DD18B CRC64;
MAALAVLRYA GSSPLLWGWG PILFGLLGSV FVLLLPLVGI EEQCCATLKG LALLRCQMWG
GIQRPVVHTT SLAVPFTALD LLPQKVKPSK ETQLEAKAAL QQALEMKKSG KREKAHKLLV
HALNMNPEFV EALTELGTIL EEEKDVVQAD HLYTKALAIS PCHEKALVSR DRTLPLVEEI
DQRHFGIIDG KVRRLMSIPK GNSALRRVME ETYYHHIYHT VAIEGNTLTL SEIRHIIETR
YAVPGKSLQE QNEAIGVDVA MKYINTTLLS RDGAITVNDI LEIHRRVLGY ADPVEAGRFR
VNQVFVGHHI PPHPQDLDKH MQELVQWLNS EETLHLHPVE FAALAHYKLV YVHPFVDGNG
RTSRLLMNLI LMQASYPPIT IRKEQRAEYY AALDTANEGD VRPFIRFIAK CTEMTLDTLL
IATTEHAVGL PGASNHACPD CKQTIPVHS
