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Q6AY47 (FICD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenosine monophosphate-protein transferase FICD

EC=2.7.7.n1
Alternative name(s):
AMPylator FICD
FIC domain-containing protein
Gene names
Name:Ficd
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins By similarity.

Catalytic activity

ATP + [protein] = diphosphate + [protein]-AMP.

Enzyme regulation

Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-234 binds ATP and competes with ATP-binding at Arg-374, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-234, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain By similarity.

Subunit structure

Interacts with HD By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Domain

The fido domain mediates the adenylyltransferase activity By similarity.

Sequence similarities

Belongs to the fic family.

Contains 1 fido domain.

Contains 2 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Adenosine monophosphate-protein transferase FICD
PRO_0000317303

Regions

Transmembrane24 – 4421Helical; Potential
Repeat106 – 13934TPR 1
Repeat140 – 17334TPR 2
Domain285 – 420136Fido
Nucleotide binding260 – 2612ATP By similarity
Nucleotide binding368 – 3703ATP By similarity
Motif230 – 2356Inhibitory (S/T)XXXE(G/N) motif

Sites

Binding site2341ATP By similarity
Binding site3741ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AY47 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: CA59D9A4F7D559F9

FASTA45851,754
        10         20         30         40         50         60 
MILMPMASVV AVAEPKWVSV WGRFLWMTLL SMALGSLLAL LLPLGAVEEQ CLAVLRGFHL 

        70         80         90        100        110        120 
LRSKLDRAQH VVTKCTSPST ELSVTSRDAG LLTVKTKASP AGKLEAKAAL NQALEMKRQG 

       130        140        150        160        170        180 
KRGKAHKLFL HALKMDPGFV DALNELGIFS EEDKDIIQAD YLYTRALTIS PFHEKALINR 

       190        200        210        220        230        240 
DRTLPLVEEI DQRYFSVLDS KVRKVMSIPK GSSALRRVME ETYYHHIYHT VAIEGNTLTL 

       250        260        270        280        290        300 
AEIRHILETR YAVPGKSLEE QNEVIGMHAA MKYINSTLVS RIGSVTIDHM LEIHRRVLGY 

       310        320        330        340        350        360 
VDPVEAGRFR RTQVLVGHHI PPHPRDVEKQ MQEFTQWLNS EDAMNLHPVE FAALAHYKLV 

       370        380        390        400        410        420 
YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSEYY HVLEVANEGD VRPFIRFIAK 

       430        440        450 
CTEVTLDTLL LATTEYSAAL PEAQPNHSGF KETLPVRP 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC079197 mRNA. Translation: AAH79197.1.
IPIIPI00371233.
RefSeqNP_001010946.1. NM_001010946.1.
UniGeneRn.162153.

3D structure databases

ProteinModelPortalQ6AY47.
ModBaseSearch...

Proteomic databases

PRIDEQ6AY47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000892; ENSRNOP00000000892; ENSRNOG00000000703.
GeneID288741.
KEGGrno:288741.
UCSCRGD:1359391. rat.

Organism-specific databases

CTD11153.
RGD1359391. Ficd.

Phylogenomic databases

eggNOGCOG3177.
GeneTreeENSGT00390000008873.
HOGENOMHOG000008059.
HOVERGENHBG095654.
InParanoidQ6AY47.
OMAMKYINTT.
OrthoDBEOG4RR6HD.

Gene expression databases

GenevestigatorQ6AY47.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR003812. Fido.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF02661. Fic. 1 hit.
[Graphical view]
SUPFAMSSF140931. SSF140931. 1 hit.
PROSITEPS51459. FIDO. 1 hit.
PS50005. TPR. False negative.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio628637.

Entry information

Entry nameFICD_RAT
AccessionPrimary (citable) accession number: Q6AY47
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2004
Last modified: March 6, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families