ID A5DNI6_PICGU Unreviewed; 1176 AA.
AC A5DNI6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGUG_04837 {ECO:0000313|EMBL:EDK40739.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40739.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40739.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
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 -!- 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; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; CH408160; EDK40739.2; -; Genomic_DNA.
DR RefSeq; XP_001482882.1; XM_001482832.1.
DR AlphaFoldDB; A5DNI6; -.
DR STRING; 294746.A5DNI6; -.
DR GeneID; 5124809; -.
DR KEGG; pgu:PGUG_04837; -.
DR VEuPathDB; FungiDB:PGUG_04837; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_22_0_1; -.
DR InParanoid; A5DNI6; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT DOMAIN 529..706
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 731..877
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 32..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 132375 MW; B1BABDE0F7DDF1E6 CRC64;
MANNFQVHMA WFQRSSPHIP SRDTAGVLFR RDLDSPSSST RPNYPIIPTT PQDPTSSIRS
SVPSSTYQST HSVLVGDKVP GSTKRASESA EMTNKRPKMG IEHGENSTFS SNFQPLKPMD
TNRDIPIKTS QRSRLSSHSS QPGAGNLQKY IGLQTKLISL LKNKLSIVES SSISQDDKEK
YIKTVYEPQA SALESSLAEL ASSTRINESS DQPEKAYEQI DFCSQFSEDE MGRMADEARE
IERPRHDQHQ QNLVEAREVV QRMRYEARAE HTNDQNYPPN GHNFPRNGQN YPRNDQNFPH
NDRSPLNVSD SPLNGPSNRA GSDEEDNFGE RTMDGLYSSE VDDNYSDLES FIDDDEVSVD
GTYRESNNPT QVTEEDSQNV ALVDEISDNS DLEEIEDFTV QLNEERELQD HDVIEISSGE
EDDLVPIPPI KSEPMAPTKN PVAASKKPVL PAQINPVSST VLSDLESDLD FSDEDLCAIP
DSIFPVPAAQ ATAGKKLPPG SEPFIKEVYS ILQSTFNLSS FRPNQLEAVT ATLQGKDTFV
LMPTGGGKSL CYQLPALVTS GRTRGTTIVI SPLISLMQDQ VQHLLDKNIR AGMVSSKGTA
SERKQTVELF RSGQLDLVYL SPEMVNASSQ IQNIISRLNS NQQLARIVVD EAHCVSSWGH
DFRPDYKGMN MFKQQYPNIP LMALTATANE KVRMDIIHHL NMTEPVLLKQ SFNRTNLFYE
IKRKNGNYLE WIRDYIVAKY AHNTGIIYCH SKQSCEQTSE KLNMWGLKTS FYHAGMGPTE
RFDIQKKWQD GSVKIICATI AFGMGIDKPD VRFVIHLFIP RSLEGYYQET GRAGRDGKPS
ECIMFYSYKD ARSLQSMIQR DSDLDRESRE NHLNKLRQVV QYCENTTDCR RKQVLHYFNE
HFDPLQCSKK CDNCANSDTV TSVERDITLF AKDIISLVSE IQRDKVTVLL CQDIFKGSNS
SKITKPGYNR SPYHGKGKTL DKLEIERIFF HLLSENCLEE YSVMRAGFAS NYVRVGRAAS
MVTSGQKRVK LVFTEQVQTS IRAGSLTESF VSAREIAERQ ASLRQDINCD PHFNKLSSIR
DNLNLTISNA SLKEMVLLLP TSKKDFLKVG GITKDQAQDF VHFKKALAAI KREKNGGKSS
QSSTSQSSRG QKSNRVHKPS QRRSQVPKTQ FRSMPL
//
