ID A0A2N5UAB4_9BASI Unreviewed; 982 AA.
AC A0A2N5UAB4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=PCANC_12247 {ECO:0000313|EMBL:PLW34673.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW34673.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW34673.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW34673.1};
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:PLW34673.1}.
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DR EMBL; PGCJ01000272; PLW34673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5UAB4; -.
DR STRING; 200324.A0A2N5UAB4; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT DOMAIN 12..291
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 292..630
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 533..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 982 AA; 109221 MW; FEB44F45BC3BD38E CRC64;
MDEDEENKWL SCLNANQLNA VQQPSNISLQ ILAGPGSGKT RVLTYRIAYL LRNCRISPDA
LLAVTFTNKA AKEMQFRLAA LIGAPLASEV TLGTFHGMCV TFLRKHGAKI KLRSNWVICD
RDQQLQYAKT TLRDHQFAEQ LQDGSVKPKT VVEEVSKAKS QGFTPQIMLR RAETSFQKLM
AILYQSYSDL LSADNCLDFD DLLLLGEELF RSHPDVISHI QHVLIDEFQD TNTIQYEIMR
LLAHRGAVTI VGDPDQGIYG FRYAQAINLE KMTQQFPGTK VAMLEENYRS SSSILKASLA
VVQQDQGRIE KNLYTSHPQV GSPMARPFRN PMEEADFIAQ EIHRLVSHTG GQLDYNDFCI
LMRYNALSRN LEAALKTARI PVRMIGAQKF FERAEVRDII AYLQLADNPI FAPAFERVIN
TPRRKLGLAA ITAVKTASQT HKISQMEVLV RAVRGKHFDG IQPAQTSTFK NFLSVITSIQ
ALAQEGTPVA ELIDHVVERI NYTDHLQKTY GPDAVQREQN IQELKAFATH LAKESQATSQ
FPPSSATDGV DQSTSKPGNR SHFTMSDRAL DRLASMFKEN DSLPDDIEEV TPLRRFLVES
SLSTDADTQE SKDDNSQPRV NITTCHSSKG LEWPVVFVVA VEDGIFPFYR CSEPDEVKEE
RRLLFVAMTR AQGLLYLTYS VERMQGAETR MQEVSSFLKK LIKPSTDAAL VDRVLTPNPP
ELDPNMRQEL STVIGRPVAS DDAVKSKIEE YESRERKTFS VPDPNNIRSS YPSSSQESKS
NFNRWGNNRG QGSLGRFSSS SAGKIPPRGV FRTASGPPTF TTAGQYNSNG GVKPSVAALS
KSLGKFSTPT PKPLCPSNQQ ARTEMLHKPF VPPMSQGYTR KPAAVNTEPP PASCPPKNPV
NGNVRLDALK AQATEFIADL KNQVPEGLFD DMSDYDETAK LDPSTSNPDA DTGPARKRRK
AAARPAKPRT APTRVSTRKK SS
//
