ADPRH_DICDI
ID ADPRH_DICDI Reviewed; 392 AA.
AC Q54H71;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ADP-ribosylhydrolase ARH1 {ECO:0000305};
DE EC=3.2.2.19 {ECO:0000250|UniProtKB:P54922};
DE AltName: Full=ADP-ribose-L-arginine cleaving enzyme;
DE AltName: Full=[Protein ADP-ribosylarginine] hydrolase;
DE Short=ADP-ribosylarginine hydrolase;
GN Name=adprh; ORFNames=DDB_G0289675;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Specifically acts as an arginine mono-ADP-ribosylhydrolase by
CC mediating the removal of mono-ADP-ribose attached to arginine residues
CC on proteins. {ECO:0000250|UniProtKB:P54922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] = ADP-D-
CC ribose + L-arginyl-[protein]; Xref=Rhea:RHEA:14885, Rhea:RHEA-
CC COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29965, ChEBI:CHEBI:57967, ChEBI:CHEBI:142554;
CC EC=3.2.2.19; Evidence={ECO:0000250|UniProtKB:P54922};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P54922};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P54922};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54922}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000148; EAL62549.1; -; Genomic_DNA.
DR RefSeq; XP_636047.1; XM_630955.1.
DR AlphaFoldDB; Q54H71; -.
DR SMR; Q54H71; -.
DR STRING; 44689.DDB0238599; -.
DR PaxDb; Q54H71; -.
DR EnsemblProtists; EAL62549; EAL62549; DDB_G0289675.
DR GeneID; 8627257; -.
DR KEGG; ddi:DDB_G0289675; -.
DR dictyBase; DDB_G0289675; adprh.
DR eggNOG; ENOG502QPMI; Eukaryota.
DR HOGENOM; CLU_047061_0_0_1; -.
DR InParanoid; Q54H71; -.
DR OMA; ACWWGAM; -.
DR PhylomeDB; Q54H71; -.
DR PRO; PR:Q54H71; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..392
FT /note="ADP-ribosylhydrolase ARH1"
FT /id="PRO_0000328209"
FT REGION 125..127
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 192..194
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 309..311
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT REGION 315..316
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54922"
SQ SEQUENCE 392 AA; 44362 MW; B99C7063F05AB67C CRC64;
MFHKFISTLT NKKITQTIMG TINKENIKPA MLLSAFGDAC GYKNGIWEFE KSPSRIYEHY
EYLGGYKNLK INKKDWRLSD DTIMHIATAI AITRPTNTDN ESICKELAKA YIHSMEDMAG
RAPGIQTINS VSLMTQTGMR SKVYQWNEID FSDRAGGCGG SMRSMCIGFK YWSDEQLDTL
IELSIESGRI THNNPVGFLG ALVSALFASY AIRSIPPKTW PLKLMTEVMP KAREYLEKTS
NSSNRNIENY EKGWNYFWNS WKSYLKLRQI PSNPDELKAA NDKGIDYPVF PKDYSDYKVR
ENFYHSISFS GWGGSSGHDS CIIAYDALLG SADNWEEMIK RSVLHGGDND STGAIGCCWW
GALYGFNGVP ECNYEKIEYK SIIEGLAKEI SN
