ID A0A0C9MW72_9FUNG Unreviewed; 969 AA.
AC A0A0C9MW72;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=MAM1_0121c05865 {ECO:0000313|EMBL:GAN06383.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06383.1};
RN [1] {ECO:0000313|EMBL:GAN06383.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06383.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; DF836410; GAN06383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MW72; -.
DR STRING; 91626.A0A0C9MW72; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000053815; 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; 2.
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:UP000053815}.
FT DOMAIN 16..301
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 302..757
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 969 AA; 110333 MW; 5D5056E9ECA4E091 CRC64;
MEEERRWRKQ FQDTINSLNE NQRRSVLSKA KTLQILAGPG SGKTRVLTCR AAHFVLNEKI
KPQQIIVVTF TNKAANEMKK RLYTMIGSKN TNNLVIGTFH AICARLVRFN AGVVDLKSNF
TIADTDVSHD IIKSLQKDRS LPISDFTRHK QKPGAIFGII SKAKSEGITA PEYSKLNSHK
FERKDIATIY TAYEEQLKLN NLIDFDNLLI KACELFRKKK NVLAHIKGVL VDEYQDTNIV
QYELIKLITK NQDTDKTVTI VGDPDQSIFS FRSAEPKNFN KMHTDYSDTQ TINMEQNYRS
TGTVLDSALH VIKQDIKRID KSLYTNNPVG IPISLISTHN EDEQATFVAK EIKKVIKYSK
GLLDYKDFAV LMRMNYISQK FEATFRKYRI PFTIIGGDRF FNRIEIKDIL AYLKFAYNNF
DYLSYSRIVN VPKRGIGDVT LTKIGAFHEA QPGNSMLETL RAIGNGGGTF SNPIRQKLKS
LAMICNDIKA MIDQKMPIHE ILEFITDAIK YKEHLKEKYF ADHEARWNNI GELISLAKAE
TYLGEDDEPV MSQTQTKKSQ AQQDQTTKDL DDLQMIDAEV VSEDDSDGEG KYFNVSELSF
GEHVADAGCM LDKVEKDAGK VFPDDQDFPE SPGDDKTTHK IAAHDEDLPE FDILDESIPD
FTSYFSDKEI DLTNITEEKE KESFHFTQKE YDQTEGSDNV KKEKQEENFS SQFPNYQHEM
DPIIEFLEYC SLSANQKEQD EAEGGRVTVS TMHASKGLEW PCVFVVTCCE GVVPMHHDPD
VSEEGRLLYV AMTRSQFFLY CVTPKERTVW GQMQTSERSR FFKGMDSKLY TTHSPEWTNE
TRSMLAVTIG KPAPPDDDNL VTTRKKSGSK KTADYSTQYT DYQSQGFYSQ SQTSQPSFPS
SPVKNESKPF YNGFVSASTI PDVKPSTRPT KRRSQQDKGQ KKKRTTAFAS QPKGKAEPSV
KPEPVDKLE
//
