ID A0A163MD02_ABSGL Unreviewed; 1014 AA.
AC A0A163MD02;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=ABSGL_09471.1 scaffold 11253 {ECO:0000313|EMBL:SAM03629.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM03629.1};
RN [1] {ECO:0000313|EMBL:SAM03629.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM03629.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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; LT554210; SAM03629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163MD02; -.
DR STRING; 4829.A0A163MD02; -.
DR InParanoid; A0A163MD02; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000078561; 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; 2.
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:UP000078561}.
FT DOMAIN 103..384
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 385..677
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 833..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1014 AA; 114790 MW; 25531B65E3E93EC7 CRC64;
MQKANVSDDK AKMDKVVNEE TSRAFAVQGL CIEGEPSVVR CQCRWKEESV PLQLPQAAFE
NRRGWKSLGA PSPNLRENCS FYFSFFNPTH FTSSNMGNSD YINQLNEYQK EAVTAEDKYL
QVLAGPGSGK TRGKVAWLIK EKNVRPSSMV VVTFTNKAAK EMKERLEDPG LLGGSRTNLL
RMGTFHSFCC RMLQRHLDWT PLKKGFGIAD ATKSKHLVEL VFKELKPQLS KFGQTKKPAE
FYGYISKAKN QGIDHVEYMA TCGQEYTTRD TALIFKAYEE ELESSNLVDF DGLLLFGRNL
FKNYPASVNF VDQVLVDEFQ DTNDLQYEIL WHLTQRGRKA LTVVGDPDQS IYGWRNANKE
NFDKMEADYK VTRVVDLKEN YRSTKNIVRG AAYVVETDRK RKPRELFTNN HSGTPISVLR
GSTELDEAAV VVAEIKRIIK YSNGLVKYKD IAILFRMNFL TLNFENALNH AKIPYVLVGG
TRFLDRMEVK DILAYLSFFH NPRDVSAFIR MINVPKRGLG DVAIKKIQMT ARMEQWTLLE
TMENLVAGHP QTASIRLMAR SRSSLQSLLV LYNEVKEQIF RKDSPGKILR WIVDAIGYME
HLKGNYTKDF ESRQANVEEL ITFANRSGEN SGESDDESGT DYIGRFLESC TLSGDAKEHE
EAKDGRISLI TIHSAKGLEW PCVFIAGCES GLIPMSRAED QTEESRVMYV AMTRAKCFLY
CTLAAERKRW DGSQPTTLSP YLINLPESRF QKRTPAWNAE VRKWIAGMLR IPYEEDEKLR
LENAGSYIYE EAESGYYDDY DDFDDYNDFN SFNDFGRLDR SCGYGNPRYT ASVAPTKTST
QYPNPAPKAK SATTPLHKVK KEMAGAASAY SILRQQVKQE VKSEHPSAYD IKPNQRALDA
ALRDHNTGHT VKREGSSSSS SKMHSAKKRK SATPALDFDQ CVSRGLQAVG TVKSSFSLDE
AISAVKTQTQ QNQYGESSAD TIKNQTIGQL DKLVDGGSLV RVKKEDGFRY YVAE
//