ID A0A2N5W3W9_9BASI Unreviewed; 1223 AA.
AC A0A2N5W3W9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PCANC_01280 {ECO:0000313|EMBL:PLW56912.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW56912.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW56912.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW56912.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW56912.1}.
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DR EMBL; PGCJ01000016; PLW56912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5W3W9; -.
DR STRING; 200324.A0A2N5W3W9; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
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 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; 2.
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:UP000235388}.
FT DOMAIN 468..648
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 670..822
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 135209 MW; 54A4B8EEAC486FA0 CRC64;
MTFAFRDDSQ QKPVGLNRFS SNINSNSKSM SHEPSTKRPP PSDHQPTASI KKPRPTPPIQ
TLHAEATADH QAMFPDECEI DFLEQLHQAE HSRSSKPSHQ QLNPTSRTQA APMRPSNSNN
STHTTPSDPD HRPAPSLPTR AYVEPSIQEM DLETLYNKRH TCISKIVVTL ENMLSIFQTG
ECSTGDDLGC LAHTKAYLDG RLAEFNAEVK RRQSSENNAL EASKSSVALI HTNQVSTHTI
NRVAPIVTTS PSPCSRLSNE NLVLAVKPLP SSEHHTPKIT HRSVSDNIQS SIKFQPNNSA
SKPAPLEKPV ASTSLLKTYQ PSTSVNHSQR TLNQAEDSCR DDPVQEASHN SIDPDLFEGI
FSADEEEDEP VPYELGDDDP DILDQTDHSL LHAPSGSIDI IRPITSKTST NPSHKSNATQ
NAASITHVPP PEEDLSKKMN HPWSRDVGKA LVHVFKLRSW RHNQIDAINT TLSGKDCFVL
MPTGGGKSLC YQLPAVVRSG VTKGVTIVIS PLISLITDQV QALCAKHIGA AAFTGTMTSV
ERDYVTNDLR SVDPALCLVY VTPEMIMKSE YLYGILTDLH NRKLLARFVF DEAHCVSQWG
HDFRPDYKGV GPKLRKDFKN VPFIALTATA NHQVQQDVMS NLKITGCRVL TQSFNRANLR
YEVRPKTKDV LQDLIRIITV DHHGESGIVY CLSKKQCEEV AAHLSMKNQV KAHHYHAGMS
KDDRQKIQQG WQVGKLQVIC ATIAFGMGID KPDVRFVVHH SMPSSLEGYY QETGRAGRDG
QISECILFYA YRDYTTFMRM VEKTTNSRDQ VERQQANAKK VVGFCLNKVD CRRSLILSYF
GEKFSADRCG KTCDTCMNPE KVVKKDVSQL MKAVVKLVKQ ITADQSESVT IAHMVDVFRG
SKSKKVTTAG HDRLEGAGQG SVLDRTDCER LLHLMVSDDI LNERFESNAM GFTNAYVQLG
STYRQFLNSQ KPVMMHFNAG VAGPSKRSAP AEPPKKVTIR SRKGGEKEAS GMEDSGSDVQ
VDDSIDQDTL VSVPRATSSQ HGPPVRGAVK QQALASLKAK RQLNEIKSTG NSSAEDCYNA
LLLLKDALSG DDDEVEFPTQ EVLQTIACLH PTSMQELGQV EGFSKRCLDQ YGQPIMRVLN
KFNTHDSATQ NKSGPQEGKS TNLTTNRPVD FQQHLSKYAA SNKQQAPKPS ANPKNKSTNN
FKKFVPRTAG SGSAAIKPMP IPR
//
