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Database: UniProt
Entry: C4XWL2_CLAL4
LinkDB: C4XWL2_CLAL4
Original site: C4XWL2_CLAL4 
ID   C4XWL2_CLAL4            Unreviewed;       964 AA.
AC   C4XWL2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=DNA repair protein RAD5 {ECO:0000256|ARBA:ARBA00013412};
DE   Flags: Fragment;
GN   ORFNames=CLUG_00335 {ECO:0000313|EMBL:EEQ36212.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36212.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ36212.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36212.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; CH408076; EEQ36212.1; -; Genomic_DNA.
DR   RefSeq; XP_002619176.1; XM_002619130.1.
DR   AlphaFoldDB; C4XWL2; -.
DR   STRING; 306902.C4XWL2; -.
DR   GeneID; 8500065; -.
DR   KEGG; clu:CLUG_00335; -.
DR   VEuPathDB; FungiDB:CLUG_00335; -.
DR   HOGENOM; CLU_000315_2_5_1; -.
DR   InParanoid; C4XWL2; -.
DR   OMA; CILFSQW; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          532..724
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          892..939
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..194
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         964
FT                   /evidence="ECO:0000313|EMBL:EEQ36212.1"
SQ   SEQUENCE   964 AA;  110495 MW;  845EB70EF26154AC CRC64;
     MHIYLEQRDV LTPPSKLFAS LKFMEGKKRF FPSPSRSPNP AETVPSKEAL FVEDEDEILE
     VEPHQASQAT RNGSAQQLSV DVPQTVPRRE PLPNNLEAPT PAEPSLSDIG FELFQSQLSS
     VIGDASMKAM RHLYAKYFNR PNYIQLASNE YFNGISFDDE SSGEASENVQ EDKREELKQV
     MERMNTEARN EAEMKKAMGW KRYIGTLDVQ AWATRPYLRS LRYQQELQLK RLIPNKMKKS
     SIVASKFGDS AVIRLYTSEA DGSREIGRLP EDITRILSPL IDLEIANFSA SVIMETKGRL
     SIGDPFFLQI KCYLNNNTFV DHGQVVGEEE NSQSKRRKTA KLGITFSQET EAEAALRLKQ
     KSISRLFDKL SIIPYDKSSV NTDAEEIPDD DSSVSSTPKP EIAPTEELSL EQLKQFYTAN
     QQSDFLENLP ETTTPPEENF ALTLRPYQKH GLSWMLSREK ELDLLEELSV NNSEVLSTQK
     RQAIRNQDDE VMDPLWSTFK WPQDPANPDL STSESEFFYA NLYNGELSTE KPVLKSFLKG
     GILADEMGLG KTISTLSLIH SVPYDSATAR TGTRNYASKT TLIIVPMSLL SQWKKEFDRS
     NKNSNHRCHI YYGDSVQTDL SLLLCNRSEN IPIVLLTTYG TVQSEWTRIN KLRDANGKLP
     KIGLFSVEFF RIVVDEGHNI RNRTTKTAKS VHELESRRKW ILTGTPVVNR LDDIFSLVKF
     LRLEPWSNFS YWKTFVTLPF EQKKFQQTLD VVKSILQPIF LRRTKNMKQK DGTPLIDLPS
     KEVVVEELEF SDREQLFYDF FKSRAYNSFK EGLKSGELLK KYTQILTHIL RLRQVCCHPD
     LVAASSELDD SWKEELAAFE EPIKKEKFWS ETMMKEKLYS LYAKVHIEDS ECSICTQAPI
     SIGELTLTEC GHQYCFHCIL EHIEFQTNNG SEPLCPDCRH PISKYRLFKV LSKSTSKKKI
     RSTR
//
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