ID A0A445EN43_ARAHY Unreviewed; 2424 AA.
AC A0A445EN43;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=Ahy_A01g001332 {ECO:0000313|EMBL:RYR76782.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR76782.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR76782.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR76782.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|ARBA:ARBA00035116, ECO:0000256|PROSITE-ProRule:PRU00657}.
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:RYR76782.1}.
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DR EMBL; SDMP01000001; RYR76782.1; -; Genomic_DNA.
DR STRING; 3818.A0A445EN43; -.
DR Proteomes; UP000289738; Chromosome a01.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0000347; C:THO complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd18034; DEXHc_dicer; 1.
DR CDD; cd19869; DSRM_DCL_plant; 1.
DR CDD; cd17756; MCM5; 1.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 2.170.260.10; paz domain; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008048; MCM5.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR14950:SF15; DICER-LIKE PROTEIN 4; 1.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF03368; Dicer_dimer; 1.
DR Pfam; PF14709; DND1_DSRM; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01661; MCMPROTEIN5.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00350; MCM; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022759};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00657};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 57..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 400..554
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 581..671
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 876..976
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 990..1172
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1235..1342
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1369..1435
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1534..1610
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1982..2188
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 665..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2424 AA; 272839 MW; BCCE8E1B115D38F6 CRC64;
MPDGESSSAT SSPELEPHLS VAEYLLQNLS LSEVKDHDDQ AVQKDPRKIA RRYQLELCKK
ALEENIIVYL GTGCGKTHIA VLLMHAMGHL IRKPQKNICI FLAPTVALVH QQAKVIEDST
DFKVGTFCGS SKRLKRHHDW EQEIGQYEVL VMTPQILLHN LSHCSIRMDM ISLLIFDECH
HAQAKSSHPY AEIMKVFYKN SFKSVPRIFG MTASPVVGKG ASNEANLSKS INSLEQILDA
KVYSVEDREL QSFVTNATIS VYHYSSVANG TDSLYTTYHA DLDLIKYQCI ASLGRNVEDH
QKRVNTKKLL NRIHENVVFC LRNIGIWGGL QASHILLRGD RSERHELVEA EGNSSDDSVC
DKYLSQAAEL FNSRLKGDGV SDLSSMEIMR EPFFSSKLLR LVQILSSFRM QQNPKCIIFV
NRIVTARSLS YILKKMKLLT QWRSDFLVGV HAGLKSMSRK TMNIIVEKFR SGELNLLVAT
KVGEEGLDIQ TCCLVIRFDL PETVASFIQS RGRARMPQSE YAFLVDSDNK KDLDLIDGFE
KDECRMNMEI ADRTSTETYI IPEERIFRVD SSGASVSSGY SISLLHQYCS KLPHDEYFDP
KPSFYYFDEK DGIVCHIIFP SNAPIHLIVS SPQLSMEASK KDACLKAIQE LYEKGSLSDC
LLPKQETTEP EEKDSSPSNT DGCEDDKSRG ELHQMLVPSP FRKSWINEEK IVHLNSYYIK
FRPFPEDRVY KKFGLFIMTC LPAEAEKLEL DLHLAHGRSV KSTFVPFGVV EFDKDEIKMA
EHFQEMFLKT ILDRSEFVSD LVTLGKGAES HNDSSTFYLM LPVVLQEYEN IMTVDWKTVR
RCLCSPIFKS PPDAVDQKPC PSDSSLQLAN GKRSIRDVEN SLVYATHKKL FYFVTNVNHE
KNGLSPSKDS GTSSYADDLL EKFSIHLKHP EQRLLHAKPV FNLHNLLHNR KYEDTEPQEL
EEFFVDLPPE LCELKVVGFS KDMGSSISLL PSVMHRLGNL LVAIELKQML SRFFPEAAEI
NSHTILEALT TEKCQERFSL ERLEVLGDAF LKFAVARHFF LTYDSLHEGD LTARRSNVVN
NSNLYKLALK RNLQVYIRDQ AFDPCQFYAF GRPCPIVCNN EMEESIHSCL NSVKEQGSST
EIQCNKNHHW LYRKTIADAV EALVGAFIVD SGFKAAIAFL TWLGIQVGFE ASQLINVCRG
SVGYIPLSAD VNILSLEDKL GYHFIHKGLL LQAFRLEFLG DAVLDFLITS YLYSAYPKLK
PGQLTDLRSL SVNNKAFACV AVDRSFDKFL LCDSSNLSEA VKKYVDYIRR PLSSNVNEGP
KCPKALGDLV ESCVGAILLD SGFNLYKVWE IMTSFLDPIM KFSSNLQLSP KRDLQELCQS
HNLDLQLQPS KLTKMFSVEA KVIVNGTCQT AVATGQSKKE ATRIASQKLF SELKAQGWRP
RSKPLEEVLK STFKGEAKLI GYNETPIDVT AINSIEHVMV NGNLSSNSNP IIRPLREVIG
IKPVDQKVQH SSKGQPSGTY DNRDCAGDLS RTGTARSRLY EFCTASCWKP PTFECCYEGG
PDHMKLFTYK VTLDIEESPD VIYEFIGEPK PKKKDAAESA AEGVFWYLER TDPNSKTLTN
SHTKRERERE RERERERERE RERERERERK REGAYNRWDE GAVYYSDQAH SWHDGNRPGD
PDATASNHTI QQKFKEFIRN FSKNGLFPYR QNLLDNPKFL LVRFEDLDEF APELSPKLES
SPADFLPLFE SAAAQVLGSL KTKVTGDTGE LEDQVAGDVQ ILLTSDKDPV SMRSLGAQNI
SKLVKIAGIT IAASRTKAKA TYVTLVCKNC KKGKQIPCRP GLGGAVVPRS CDHIPQAGEE
PCPIDPWLVV PDQSQYVDQQ TLKLQENPED VPTGELPRNL LLSVDRHLVQ TVVPGSRLTV
TGIFSIFQAS NSASNKGAVA VRQPYIRVVG MEDTNEAKSG GPSAFTPEEI EEFKKFAAEP
DAYKNICSKI APSIFGHDDV KKAVACLLFG GSRKNLPDGV KLRGDINVLL LGDPSTAKSQ
FLKFVEKTAP IAVYTSGKGS SAAGLTASVI RDTSTREFYL EGGAMVLADG GVVCIDEFDK
MRPEDRVAIH EAMEQQTISI AKAGITTVLN SRTSVLAAAN PPSGRYDDLK TAQDNIDLQT
TILSRFDLIF IVKDIRIYSQ DKIIASHVIK VHASADATAS ENRVSKEENW LKRYLHYCRT
ECHPRLSESA ATLLQNNYVK IRQDMRQQTN ETGEAAAIPI TVRQLEAIVR LSEALAKMKL
SHVATEEHVQ EAIRLFTVAT MDAARSGIHQ QISLTPEMAN EIKLAETQIK RRIGIGNHIS
ERRLIDDLNR MGMNESIVRR ALVIMHQRDE VEYKRERRIT LIPLVVNLVN SLNLNSSFII
IYLNDLDLKN IELKSKTEKI VYKY
//
