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Database: UniProt
Entry: A0A420JB23_9PEZI
LinkDB: A0A420JB23_9PEZI
Original site: A0A420JB23_9PEZI 
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
//
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