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Database: UniProt
Entry: A0A251K0S2_MANES
LinkDB: A0A251K0S2_MANES
Original site: A0A251K0S2_MANES 
ID   A0A251K0S2_MANES        Unreviewed;      1230 AA.
AC   A0A251K0S2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=MANES_10G122800 {ECO:0000313|EMBL:OAY39797.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY39797.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY39797.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY39797.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; CM004396; OAY39796.1; -; Genomic_DNA.
DR   EMBL; CM004396; OAY39797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251K0S2; -.
DR   STRING; 3983.A0A251K0S2; -.
DR   EnsemblPlants; OAY39796; OAY39796; MANES_10G122800.
DR   EnsemblPlants; OAY39797; OAY39797; MANES_10G122800.
DR   Gramene; OAY39796; OAY39796; MANES_10G122800.
DR   Gramene; OAY39797; OAY39797; MANES_10G122800.
DR   OMA; VNWSDHA; -.
DR   OrthoDB; 1114285at2759; -.
DR   Proteomes; UP000091857; Chromosome lg10.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF153; ATP-DEPENDENT DNA HELICASE Q-LIKE 4A; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 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; SM00341; HRDC; 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.
DR   PROSITE; PS50967; HRDC; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857}.
FT   DOMAIN          466..641
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          666..816
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          681..723
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          1025..1107
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          102..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  138486 MW;  815925F3111D3A78 CRC64;
     MRKNLSNSGQ DNKCNEKLPE VNWSQHANAH DNFSSQKKFL SSNFLFSLEG QKPCIEGSMA
     MRLTCCQIQS LQRLQSQEVE KAWHTLCTLQ ISCRNYLQPG KTGPLKNARN DSLQDVGKPT
     LHSSSNRRKD SEDMHANQNF RDSSLRNNES TRYTGNVFPQ DNARAAEAGS DMGRQNNIKG
     SAINNTQSKA FVGLMSNHIV HTKQSKESPE ALADFIDDDD LLGNIDVDQI VMEHYQSTST
     PQPSVSKFPP ITPTADKNNF MRSEETFLPS ELCQNCNHGF KLGLCPEAAN HLQEMKDMLI
     SVSNELLDNT ANLSPAQIEK LRQDRLQLNK QIQQLEKYLC DGERQNSHFS ASTATRNFQY
     ETPQSAACRI DPPRFNAQFQ LPNGPGGHEN WNLPSVSFSS VDRFGLSSGP VDREPYIPKF
     IEVNYIEGSN DPKWSSTNFS WTKKLEAYNK KVFGNHSFRP NQREVINASM SGFDVFVLMP
     TGGGKSLTYQ LPALISPGIT LVISPLVSLI QDQIMHLLQA NISATYLSAN MDWTEQQEIL
     RELCSDYCKY KLLYVTPEKV AKSDVLLRHL DSLNARGLLA RIVIDEAHCV SQWGHDFRPD
     YKELGILKKK FGKTPVLALT ATATASVKED VVQALGLVDC IVFRQSFNRP NLWYSVIPKT
     KKCLDDIDQF IKGNHFDECG IIYCLSRMDC EKVAKKLQEC GHKAAFYHGN MDSAQRAYIQ
     KQWSKDEINI ICATVAFGMG INKPDVRFVI HHSLPKSIEG YHQECGRAGR DGQRSSCVLY
     YSYSDYIRVK HMIIQGQIEQ NPWTPGYNRT NMTNSERVLE KNTENVLRMV SYCENDVDCR
     RLLQLLHFGE KFDSGNCKKT CDNCSKIKTL VEKDVTEIAK QLVELVKLTG QQFSSSHILE
     VYRGSLNQYV KRYKHETLSL HGAGKHLAKG EASRILRHLV TEDFLVEDVK KSDIYGSVSS
     VLKVNESKAY NLCSSGQTIV LRFPSAVKVS KLSKYDATPA KGTLTYGEQS PLVDAPAQPQ
     SEVDLSLSAK LYSALRMLRT ILVKEAGDGV MAYHIFGNAT LQHLCKRIPR TKEELLEING
     IGKAKVSKYG DRLLETIEST IREHHNTDKN SSGSNDSTDS IKRRRDATRA AKLNVEEEDD
     FTKSTGRSKK RAAKLQNKDT EVYNARETDQ NQCLDDDLDF EDSCYDHETN GSAVEADKNG
     TGRVLPSWST PGNKIKSSNH NLFQEYAMNS
//
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