ID A0A1D6NYF5_MAIZE Unreviewed; 1882 AA.
AC A0A1D6NYF5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=ZEAMMB73_Zm00001d045707 {ECO:0000313|EMBL:AQL03024.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL03024.1};
RN [1] {ECO:0000313|EMBL:AQL03024.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL03024.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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|RuleBase:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU363044};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000256|ARBA:ARBA00026071}.
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|RuleBase:RU363044}.
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DR EMBL; CM000785; AQL03021.1; -; Genomic_DNA.
DR EMBL; CM000785; AQL03024.1; -; Genomic_DNA.
DR ExpressionAtlas; A0A1D6NYF5; baseline.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR025476; Helitron_helicase-like.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR10492:SF94; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR10492; UNCHARACTERIZED; 1.
DR Pfam; PF14214; Helitron_like_N; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044}.
FT DOMAIN 718..899
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT DOMAIN 1643..1689
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1882 AA; 213881 MW; 036704AD15D1C013 CRC64;
MEHNADRTPL IDISNTSVTG DQIGSNSLGP IDDANERKRQ RDRERYATMS IEQKNEKNRK
RREARQRNKG LPLKSESSRG PIKNTPLAGN SIERKRQRDR ERRATMSVEQ RNEYNNKRRQ
MRQRNKGQNV MPDVSGDGDK KENVDPDDDS DWLHRNETFQ SNDYVATTDL LPPGSVHESV
GVIGEPSIGV REYRLERLRL YNQTPKRKEA KIEYMRKRRV LQADTLNVAS IAMEDPTYTP
EVVHPATEPS TVTTCDWVIP EFIRTPFLPA QTQTEDVGSF DMSTEAIRHK HHVPRGERQA
ILARRNKQFQ ASIARNVTTL NGDTIGDANN NGNYYPILNG SCTTTIPYSQ TNRVFPSAQC
SVPCQAATLP TNGSEGITEQ GNEVEHTQEK PTVISNDDDD DDEAVIFEED DDNDEGYIFA
GQYEETDEDI EIDGTQDEST GTDVPDPYDK VYSNLPEETH MLKPVPDCGY CTAKKFEYEP
PGFCCRGGKV ELAPLDTPPQ LRSMTTNVRD SGIYTFRAQG MMYHNIKSFG KEGGSEHKHL
ELYFYDDDPS LEHRYRKCRE EQLQKDKDVI KQIVGILHGN PYSEHLRSMG HVENLDDYHI
ALNLDQTLNQ KTYNTPLTSE VAAVWIEGSE RRGQFSKSVM LHGKDRSSHG IRSYHGCYDA
LSYPLFFPKG ELGWHANIPK VGVSMDEVDA YRATHRANNS NDEDAESPTH LCVSVRDYYC
YKFQIRPGVF NPILHGKRLF QQFAVDTYIK IESSRLDFIR KNQDRLRADL YQGLVDSMLD
GDIRAEKVGK RTVLSTSFIG GPRDMKRRYM DAMALVRKFG KPDIFLTMTC NPNWDEIRRE
LLPGQTPQDR PDLVVRVFHA KLQELKHRLT KQDILGKVRA YVYVVEFQKR GLPHAHFLLI
MQRKYKLTCP EQYDLLISAE IPHNKYPELR KMVIKYMMHG PCGSLNPNCP CTKGHVSCKN
HYPRPFSDTT LQGKDSYPIY RRRDDGRKEK VRGCELDNRW VVPYNPYLLR LFNCHINVEA
CGSIKAVKYL FKYIYKGHDR ASVVMRDASK ADDDVDEIKQ YRDARWVTPP EALWRIYGFE
LSQNSPPVMQ LQLHLPNMHM VAFHERQMVE RVVNRPGADR SMLTAYFEAN RLHEGARGIL
YRDFPEWYTW QSGKGKVWQR RKRDTGGQVG RIVSAHPAEG ERYYLRVLLN HVTCATSYVD
LRTVDGVPLP TFREAAERRG LLESDNTLDD CLTERALFQM PSALRRLFAT ILVYCEPSDV
AVLWQNHLDV MSEDYQHRSQ GKTHVEQMVL IDIRNMLQSM GKDIKTFPLP PIIDAYDDAI
GTAREVYEEE SIEPAVGDVA LKDSLNEEQR VAYDKILSAV DTDKGGLFFV DGPGGTGKTY
LYRVLLATLR SQGKIAVATA TSGVAASIMP GGRTAHSRFK IPLTIDDGAV CSFTKQSGTA
ELLRKASLII WDEASMTKRQ AVEALDNSMR DIMGRPELPF GGKTIVFGGD FRQVLPVVRK
GSRAQVVASS LRMSYLWESM SHLKLVSNMR AKNDPWFAEY LLRVGGGTED TNSDGDICLP
DEVCVPYSGS DNDLDNLIDF VFPNLNENMS DSTYITSRAI LSTRNDWVDM INAKMIDRFQ
GEHMLYHSFD SAMDDPHNYY PPEFLNTLTP NGLPPHVLKL KIGCPIILLR NIDPANGLCN
GTRLVIRGFQ RNSIDAEIVL GQHAGKRIFL PRIPLCPSDE EMFPFQFKRK QFPVRLSFAM
TVNKAQGQTI PNVGVYLPEP VFSHGQLYVA LSRAIARSNI KILAIPTVDG KKSGVRPFGV
SLLIAGYDDN GPQLYQVDPS GSYFSWKASA MGKNVSNAKT FLGKRYEGQI SSNNIEIGII
RADREFKVLS PSEIKDFLEE VE
//
