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Database: UniProt
Entry: E6R197_CRYGW
LinkDB: E6R197_CRYGW
Original site: E6R197_CRYGW 
ID   E6R197_CRYGW            Unreviewed;      1283 AA.
AC   E6R197;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=DNA repair protein RAD5 {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CGB_B6660W {ECO:0000313|EMBL:ADV20561.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV20561.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV20561.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(2011).
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; CP000287; ADV20561.1; -; Genomic_DNA.
DR   RefSeq; XP_003192348.1; XM_003192300.1.
DR   GeneID; 10187714; -.
DR   KEGG; cgi:CGB_B6660W; -.
DR   VEuPathDB; FungiDB:CGB_B6660W; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_8_1; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000007805; Chromosome B.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR001650; Helicase_C.
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:SF47; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          560..749
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          942..995
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1105..1259
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          61..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1283 AA;  142657 MW;  9F715F95B748B05B CRC64;
     MEDQCWKEVI LSADPFRDDG GRKEGFGSFW NYQEHCKEND HIKGRNDRCK KLGIPIQSSY
     FSAPSSSSHA SSSRTSSSLN PLSTPASSSR TNQPYAMPSA SSSKGVSKKT SRPSILDALA
     PSPTARSVHS SSPMPSPQVF TTPGTTSAAT SHNAAPHAKT IRTSASKKVY SSDTHRPASS
     KGGSRALTAS PSSSSDIVNM VEEYIANAGS STFTTFLSDR TPLAPLRQNA KGVVPKREPV
     RQRNVSGTDD DGTSLPSVIE QDMAFYQTFA PKREPIAVAA TPSVLTTGVS ASASADRTSY
     APTGLPLRDF YSLLLNELKL GRNGLGIDVI PTEDKEQRYT AELQHLLKAL AGFRDEKHKF
     RIILQRMKFL KDALCNPNTV KGYVNPPIDI TLIFPSLRSI VENGRLIMSR MMTNATGQLL
     KVPCGCGDAS HTCDLRALSK DSGILHWREP SAALHGSQSA HAGPVMPMSV GRAHATYSDD
     DMSDNDDPRD PRGLMYKYTQ SIAESLAAFF SDNLKDFHAD TDVDKALQKL GLSSLSDFLP
     GLKIKLMPHQ VLGVSFMFEK ERDQRYRGGL NGDSMGLGKT VQSIATMAAN PSQDVKCKTT
     LIVAPLALLS QWKNEIESKT TEGLMKVFIH HGPKRATTIA DLKQYDVVLT TYGTLTSESP
     SDKPSKNKVK PVDGCKEEGD IPAKKVGPLM KVKWYRVILD EAHQIRNKST RATKACWALR
     AHLRWCLSGT LVVNSLDDIY PHLHFLQISP SAQWEHFREH ISKLQKRYPK LATNRVQAIL
     RVCCVRRHKE SELNGKKLLE LPPKTTKIID LQFTDEERQI YTAIENKYKI TFNSFLRKGT
     VMKHYSIMLV MLTRLRQLTC HPWLLRRSPN DIRDVRDVVV TGNDLLAGLA APMMDDISEQ
     ARASTLIGPE YVERVKTLLE ERAKRLEEAP PDMIDEAGDG ECSICYEQYS DERITPCCHS
     FCAECLENIF NSAQGNADLS DDDVQVGRRK CPLCRSVIDK AKIFRASAFM PVGNDNEDDE
     DDDWGSQAEE VEDEVVDICA KLEELNDDDM SEKKKGKRKA VDYSLSKKKK RKFKGKDVEG
     AEDKLQDVND EVLIEDVLPS TKMKKLGELI DAIIEQDPSQ KIIVFSQFVE YIDLCSIFLR
     RRNIPHAKYV GSMKQDERED TIKNFNRPME EDKSPRCLLM SLKCGGVGLN LCIANHVICL
     DLAWNAATEN QAVDRAHRIG QTREVVVHRL VVENTIDQRL MELQQQKQAL SDGAMGEGAA
     AKLGRLNIND LIKLFGVRSH DDE
//
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