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Database: UniProt
Entry: A0A1W2TDE4_ROSNE
LinkDB: A0A1W2TDE4_ROSNE
Original site: A0A1W2TDE4_ROSNE 
ID   A0A1W2TDE4_ROSNE        Unreviewed;       998 AA.
AC   A0A1W2TDE4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=SAMD00023353_0301210 {ECO:0000313|EMBL:GAP86005.1};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP86005.1};
RN   [1] {ECO:0000313|EMBL:GAP86005.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP86005.1};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) 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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR   EMBL; DF977448; GAP86005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TDE4; -.
DR   STRING; 77044.A0A1W2TDE4; -.
DR   OMA; VDVMFHR; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000054516; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:GAP86005.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054516}.
FT   DOMAIN          314..477
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          499..674
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  112747 MW;  5A2E7A99C3A89D2B CRC64;
     MDRKEGNFSP KRRKLDFNPL RSDDRYSSLP ARSHNASRPH SRALNATSSR ASTPRNQSSY
     AATPKPDESN GPGPSVSHED QLALDRDWYG GDETGGHTFG DDSHNPFGSY DTSWVEQQQR
     EAQMVEKKAG RQMNARQLQR QKDNDAWETN RMLTSGVAQR RGLGDDFDDD NEGTRVHLLV
     HDLKPPFLDG RTVFTKQLEP VPAVRDYQSD MAVFSRKGSR VVKERRQQRE RQRQAQDATN
     MAGTTLGNLM GVKEEEGDSA LPIAAEDDQA NKGGGNKFSE VMKKNDGASN FSQSKTLREQ
     REFLPAFAVR EDLLRVIRDN QVVIVVGETG SGKTTQLTQF LYEDGYGKRG MIGCTQPRRV
     AAMSVAKRVA EEMEVKLGST VGYAIRFEDC TSKDTVIKYM TDGVLLRESL NERDLDRYSC
     VIMDEAHERA LNTDVLLGLF NKILQRRRDL KLIVTSATMN SKRFSDFFSG APEFTIPGRT
     FPVDIMFHRS PVEDYVDQAV QQVLSIHVSM GSGDILVFMT GQEDIECTCE LVRERLDALN
     DPPELSILPI YSQMPADLQA KIFDRAPPGV RKCIVATNIA ETSLTVDGIM YVVDAGYSKM
     KVYNPRMGMD TLQITPISQA NAGQRAGRAG RTGPGRAFRL FTEKAFKDEL YIQTIPEIQR
     TNLSNTVLLL KSLGVRDLLD FDFMDPPPQD TITTSMFDLW ALGALDNLGE LTDLGSKMNA
     FPMDPSLAKL LIMSEEYGCS EEMVTIVSML SVPNVFYRPK ERQEESDAAR EKFFVPESDH
     LTYLHVYSQW KSNGYSDGWC TRHFLHPKSL RRAKEIRDQL LDIMKMQKME MISCGTDWDI
     IRKCICSGYY HQAAKVKGIG EYINLRTSVT VQLHPTSALY GLGFLPDYVV YHELILTSKE
     YMSTVTSVDP HWLAELGGVF YSVKEKGYSA REKRVTETEF NRKIEIETKM AEDKRRQEEQ
     QKAEQEKSVK KPVAEKTRKI ITSGAVKKLA LKRKGRGF
//
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