WRIP1_SCHPO
ID WRIP1_SCHPO Reviewed; 504 AA.
AC O13984;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATPase WRNIP1 homolog C26H5.02c;
GN ORFNames=SPAC26H5.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16188.2; -; Genomic_DNA.
DR PIR; T38421; T38421.
DR RefSeq; NP_594449.2; NM_001019878.3.
DR AlphaFoldDB; O13984; -.
DR SMR; O13984; -.
DR BioGRID; 278572; 23.
DR STRING; 4896.SPAC26H5.02c.1; -.
DR iPTMnet; O13984; -.
DR MaxQB; O13984; -.
DR PaxDb; O13984; -.
DR EnsemblFungi; SPAC26H5.02c.1; SPAC26H5.02c.1:pep; SPAC26H5.02c.
DR GeneID; 2542096; -.
DR KEGG; spo:SPAC26H5.02c; -.
DR PomBase; SPAC26H5.02c; -.
DR VEuPathDB; FungiDB:SPAC26H5.02c; -.
DR eggNOG; KOG2028; Eukaryota.
DR HOGENOM; CLU_017985_0_1_1; -.
DR InParanoid; O13984; -.
DR OMA; RIILSQC; -.
DR PhylomeDB; O13984; -.
DR PRO; PR:O13984; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
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; ISO:PomBase.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:PomBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; ISO:PomBase.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:UniProt.
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 InterPro; IPR006642; Rad18_UBZ4.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA replication; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..504
FT /note="ATPase WRNIP1 homolog C26H5.02c"
FT /id="PRO_0000310280"
FT ZN_FING 6..33
FT /note="UBZ4-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 55..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 129..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 504 AA; 56306 MW; 4DA6DA297723D90A CRC64;
MSGPDHVQCP VCAKTVTMND INPHLDSHYS DSSGPSKPVS PFFKKERYKH HLETNVSSHQ
SATKFIEPEP SPTKKTKLTR RDTRPLAERA RPKSLDEYVG QEELVGERGI IRNLIEQDRC
NSMILWGSAG TGKTTLARLI AVTTKSRFIE ISATSTTVAD CRKIFEDSQN YLTLTGRKTI
IFLDEVHRFN RAQQDIFLPM VEKGLVTLIG ATTENPSFRL NSALISRCPV FVLKKLTRDN
VKKILNHACL LESERLGSSM PNVETSIIDY ISAITDGDAR MALNALEMSI GMLRQGPLSL
EDIKDKLVRS SALYDRVGDV HYDTISAFHK SVRGSDVDAT LYYLGRMLES GEDPLYVARR
MVRIASEDIG IADNSMLPLA SSTFTAVQQV GMPEADVILA HCAVALALAP KSVDVYRSYN
AVKSFLSSHP DAGRAEIPMH IRNAPTNLMK QLGYHKGYKY NPDYKDGLVM QEYLPDSIKG
TKFYKLPIEL KEDEEIKNLK TDTK
