ID A0A061HB88_9BASI Unreviewed; 830 AA.
AC A0A061HB88;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=PFL1_04600 {ECO:0000313|EMBL:EPQ27856.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27856.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ27856.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27856.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR EMBL; KE361637; EPQ27856.1; -; Genomic_DNA.
DR RefSeq; XP_007880317.1; XM_007882126.1.
DR AlphaFoldDB; A0A061HB88; -.
DR GeneID; 19318701; -.
DR KEGG; pfp:PFL1_04600; -.
DR eggNOG; KOG0353; Eukaryota.
DR HOGENOM; CLU_001103_12_5_1; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 150..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 409..563
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 15..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..759
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 90049 MW; 1E5B93BEEAB94E94 CRC64;
MNGPDSDVKI FHSNVGVRAN GGSGGGSSNA NGHRNGRGPP TQPTTPHTEE IYDEEVAARL
EELDDEIGEL ATRISELQRT RTRLVRERQT VYQSYIDGLD HGAAGSSSVA SAKRGTDYTR
SDFAWSTRLL ATAQKTFGIK SFRMCQEAVC NAAMDRRDAV VVMPTGGGKS LCYQLPAVLE
DGLTLVVSPL ISLMTDQVLN LREKGVECEL LSGAISREQT TDILRRVRTG DASTSTPSSA
SSAKKRKKVA GSGSRTATKD DEDEDKGDDE DDERGQGKSD GIKLLYVTPE RIAKAKNTLS
ALQKAHQQGR LSRIVIDEAH CCSQMGHDFR PDYTKLAILR NLFPDVPIMC LTATCGPRVL
KEVLEIVGLP PTTRSDNAAP RKTVYFSAPL YRSNLRYSVL TRPQSAQESM EAVRYWILER
HAGKSGIVYC LSKKDTATMA SALYELSGGR IGTAVYHADL DDAEKHQVHV DWRQGTVQVV
CATIAFGMGI DKPDVRFVLH ACISKSLDGY YQETGRAGRD GEPSDCVLFY RPQDATRVSG
LVAGEATGQE KLHAMLSYSQ SAECRKLLFA RYFKDDFGDA AACNACDNCQ EPAEVVDVKA
QARSLLRVLT YIVNKGGRVT PALLVSLAMG QKAGRFPLAQ SSSSTDKVDL KPLIGTKLAN
KDLLETAMVQ MLIRGYVEDV YHATAYTVNV YVKPGRLQGR LERDGLSVAL PRKAGGKAKK
RAKANGAKRK ASTAAEESEE DDDVVDDDDD DDPIDDNDGE EGSAPLRGGR KVAATGGGDH
EADEDEAAPL TELRKRRKLS DKLLTTASAG MRPRGASGRT HTDAIELDSD
//
