ID A0A420JB23_9PEZI Unreviewed; 2163 AA.
AC A0A420JB23;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=GcM3_003005 {ECO:0000313|EMBL:RKF84015.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF84015.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF84015.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF84015.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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:RKF84015.1}.
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DR EMBL; MCBQ01000369; RKF84015.1; -; Genomic_DNA.
DR STRING; 62708.A0A420JB23; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd18041; DEXXQc_DNA2; 1.
DR CDD; cd22318; DNA2_N-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.30.230.30; Impact, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
DR InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR036956; Impact_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR020569; UPF0029_Impact_CS.
DR PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE_NUCLEASE DNA2; 1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01930; Cas_Cas4; 1.
DR Pfam; PF08696; Dna2; 1.
DR Pfam; PF01205; UPF0029; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00910; UPF0029; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RKF84015.1};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RKF84015.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RKF84015.1};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:RKF84015.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383}.
FT DOMAIN 574..776
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 786..886
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1141..1227
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1249..1309
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1317..1543
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT DOMAIN 1921..2027
FT /note="Impact N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01205"
FT REGION 29..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2163 AA; 244654 MW; 7CD6F0B10708A9DF CRC64;
MKSDLSLIST WLDTVQPLLN MPLQRSFSDQ NHSTKLKQKW SRNRNIQRKK STDLPSNLLR
EKPPIPVSTA SRNKLSNFQF SGRVQTELKT KICPLSNDEK ENEDTRENLH IIRDHRVQKE
EREVHPTPPD KTSNKSPSTP ASKLTLPDLI CMGDVRRVRQ DISPEEKLEW DQNKGEHQNF
ALDFDAVRAV GKRAQSSSPL VSSPIQAPIQ FDPGSELWGR YSHSDLQLPT CQGLSIPSLA
HIMNKSSPKN VQEGVPLRSV SVFRRANSCG NHFPKRMKYS DIRNDDSIDP PFIDSSKVST
LIKQIKDGLA QHKKSDMIQE TTLKTNQSDF TEIPMNQETF SRIKNGPSES EFLPDYQSKV
SPSMCEHDAP DCLSSNSLNT DYGDFDEDEL DPSLLKTSKS VSKEYISNSK CKSISIGSSA
SPLNLKQQKS EMYSAQKNGI NPQQSHMAST EDLIGEFDDS EVEILSADLE FVVSQYDTRS
INEPKVLPPR HVDVKQLKDK LNIESEDEFD DGGLDDDDFK AAEASTLQTF NGLTTPQEKT
RAIQRYLVVD IMSSLYEDSG GRKKIEKILS LQIEHTKHLR SIHLRGTWVE TPVTVNAFVH
IIGLFNSNGQ CIVDDDENLL ILHPDHLISS TVVADSFSCI RRAVLQDRVK ATSQPNVSLI
YGTLLHEIFQ AALISNRWDS EWLEALTEDV AKKHVEDLYT IKLQTSEAVR DLKNKIAHLQ
SWAALFVCSN PKPGAILNTP NGETVSMCIE KLLDIEEHIW SPIYGLKGNI DATVQVIVKE
KKGQRRLIVP LELKTGKNQS ISHRAQTALY NLLLSDRYDI DIAHGILYYM ETSETQQIPT
IRHELRHMIM QRNELACFVR ERSSQLPPML KEQHKCNGCY ANVPCFTYHK LADDGTGETS
GLKSKFDQLV KHLTRQHKDF FLKWDDLMTK EEGENFKFRR ELWTMLSSER EKLGRCFSNV
IIEPGSFQEN NRNKKISRYK YTFIKKDYPS DFSFLDSQIN VGEPIVISDE KGHFALANGF
AIQASKHKIT VEVDRRLCNN RVRQAGFNEV DNQVFLSTTE VAQSGKDSIK KSSKRMSQSV
LYRLDKDEFS NGMATVRNNL IQIMADGPFG SRQIRRLVVD LEEPRFKTQV SSYKLKDYEK
INIDQKRAIE KVMCAEDYAL ILGMPGTGKT TTIVYVIQAL VSLGKSVLLT SYTHTAVDNI
LLKLKDKNIP ILRLGQLSKI CPEVTEFVTL AAEPKDSFEK IRNDWYGTPI VATTCLGINH
SIFNERTFDF CIVDEASQIT LPVCLGPIRL ARTFILVGDH NQLPPLVQNE EARKGGLDVS
LFKRLSENHP TSVVYLEHQY RMCEDIMTLS NTLIYNGRLK CGNQEIARRK IFIPSLDNLQ
HHHFPPLTSS GTDKVRCLGT NGNKCWLRDL IIPEAKVLFV NTDSLVPLSR EVAKGNRIVN
PTEANICTKL VHSLLSVGVP ASSIGVMTHY RSQLELLKYY LRAHKQVEID TADRFQGRDK
DVIILSLVRC NDARSIGELL KDWRRINVAF TRAKTKLLVI GSRETLKGDN ANTGNEEMVA
RFVKLMEKNN LVYHLPLGAL EDHFFEDGNT QATACTMDIS SSRLETLKSP GSSYDYLDQT
INSNEKKAKL KHVRKSYENQ NYPTQIQITD SISHVYIFNK SGYPKIFQKP SHMATPKDLQ
DLLRLMTGQN KNSMMEAMKR VKALQSANLS RYSFPLTIAS TDITTLKSAI GGEKAAKSLL
RACMLYIKSK EGVADKNIIE NSSKNFKRKR SQYELSDQPK TPAELEASLS LPQPSKDEET
ISRCIVYSNR APFLLAFTVQ LLKYTMPEQP LSSRLSLGQA VVNFNANKKA TSLSLRELNC
SQSLSWGPKI KIMNREVTVL KRSGYNWKGD EIKNEHEKKD DVNVKDGSKK KWNISKSMTS
KKSTFVARSI QISSPSDVGA ALEGLFSEDQ GLRGATHTIT AWRVQVGKSI SEGFNDDGEK
NGGQYLLDLL RGENLDGILL VVSRWYGGMI LGPERWKIIS EVSRDCLSQR LRINGSINQD
ALWGLNLEDN TECSIIDNVI PVFKPDKARA YLLNSFVSPP DLNFQKKKKS VIAVYREKEE
NLGLLLEAFD ILFTSWTSHL SPDELDRKAW GWYSQTRPDV EDGVMGWGAK GTVKLSDILK
LKR
//