WRIP1_DICDI
ID WRIP1_DICDI Reviewed; 876 AA.
AC Q75JU2; Q559T3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATPase WRNIP1 {ECO:0000250|UniProtKB:Q96S55};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q96S55};
DE AltName: Full=Werner helicase-interacting protein 1 homolog;
GN Name=wrnip1 {ECO:0000250|UniProtKB:Q96S55}; ORFNames=DDB_G0272158;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000305}
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: Functions as a modulator for initiation or reinitiation
CC events during DNA polymerase delta-mediated DNA synthesis. Has an
CC intrinsic ATPase activity that functions as a sensor of DNA damage or
CC of arrested replication forks and regulates the extent of DNA synthesis
CC (By similarity). {ECO:0000250|UniProtKB:Q96S55}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q96S55};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000008; EAL71231.1; -; Genomic_DNA.
DR RefSeq; XP_645251.1; XM_640159.1.
DR AlphaFoldDB; Q75JU2; -.
DR SMR; Q75JU2; -.
DR STRING; 44689.DDB0305118; -.
DR PaxDb; Q75JU2; -.
DR EnsemblProtists; EAL71231; EAL71231; DDB_G0272158.
DR GeneID; 8618418; -.
DR KEGG; ddi:DDB_G0272158; -.
DR dictyBase; DDB_G0272158; wrnip1.
DR eggNOG; KOG2028; Eukaryota.
DR HOGENOM; CLU_328297_0_0_1; -.
DR InParanoid; Q75JU2; -.
DR PRO; PR:Q75JU2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA replication; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..876
FT /note="ATPase WRNIP1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000391790"
FT REGION 56..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 876 AA; 98566 MW; 8C234DD6154E3297 CRC64;
MSKKTNINTN TKINNFFQTK TNNANVVNEK GYIEDDNEII DINDFEEDQN LYKIQNKSNG
NNSINNNNNN KNTPTKPNLN LTPTKSHTIS FPTRPKLPSF TQPNNNNNNN NNNNNNNNIN
NNNNNNNNNN NNNNNNNNNN NNNSSTNVKP TTTTTTTTTI NNNNNNNNNN NINNNNIDLK
NKYSFLTNFK KKSFAPLSEQ MRPTELSDFI GQESLLVGDP IVKKLFQSPE LPSFILYGPP
GCGKTTLAQI VASKSNYNIN ALSAVGSGVK DIKEVIDKAR NTLQFGKKTI LFIDEIHRYN
KLQQDVLLPA IESGIIILIG ATTENPSFEL NGALLSRCKV FKMEKLTKEN LETLIKRTLE
VTPLLMDRRL IMDEDAIKSL AEIADGDARV AINVLDMAIK ANKEEQTYKE RMEEKHSTSG
IVRDIVLTKK QMGSLLQRTS LIYDKGGDAF YELISALHKS VRGSDANATA YWVIRMLESG
CEPLYIVRRM VRMASEDIGL ADNSALPLAI AAYQAVHFVG MPECTNAILQ CAVYLANAAK
SNSCDHWYAH TREYLEKHEG PPVPIHLRNA PTKMMKDWGY GADYQYNHAF DDQSQVTQIY
LPEPIKNEKF FEYKLTCPSV KDRQQSQDQT QRSSQQQQQQ QTQPQQQTQP QQQTQQQIQQ
QLEQLKQIQQ QLEQQVQQQI QQQSSQSPSQ QSQLQELQQI QQQLQQIQQT NSQINNKNND
SNIIKKNVNN SLDLNPTLPK KQKMIIPSIL DNSNNNNNNN NINKSPTPIK KANISHNQLD
SSINTSAITI DDSSECDINF DDDFDMASVS STTMISNIPV GANVAGATEA ETETKAISST
DTKESVSIND SDKDLTTTHK NEQDQNNPPD PISLDF
