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Database: UniProt
Entry: E3KTK1_PUCGT
LinkDB: E3KTK1_PUCGT
Original site: E3KTK1_PUCGT 
ID   E3KTK1_PUCGT            Unreviewed;       735 AA.
AC   E3KTK1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=PGTG_13494 {ECO:0000313|EMBL:EFP87708.1};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP87708.1, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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};
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DR   EMBL; DS178308; EFP87708.1; -; Genomic_DNA.
DR   RefSeq; XP_003332127.1; XM_003332079.2.
DR   AlphaFoldDB; E3KTK1; -.
DR   STRING; 418459.E3KTK1; -.
DR   EnsemblFungi; EFP87708; EFP87708; PGTG_13494.
DR   GeneID; 10539106; -.
DR   KEGG; pgr:PGTG_13494; -.
DR   VEuPathDB; FungiDB:PGTG_13494; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; E3KTK1; -.
DR   OMA; KVKVWRH; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          70..264
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          289..466
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  82772 MW;  FEEEBE5911653D38 CRC64;
     MAKHIQFHQT DSESETQADS PSRFDSTHQP NSKAAQHQNG MTDKQRRDRS EALAQAQRQL
     PIYAGKEAII NETWNNDTIV VLGETGCGKT TQIPQYLIGP EYQKLSNNST KPIKVVVTQP
     RRVAAMSLAT RVSEEVGCRL GTTVGYTVRF DDCSEQKTRL KYVTDGTLLQ EMLSDKLLSN
     YDIVIIDEAH ERSLRTDMLL GFLKGIQRTR RTMVEEGSDF PKRKSSDSQQ GKPARALKVI
     IMSATIDAER FSQFFDDAKI LYVKGRQHPV TLFYAQEPQE DYVESAVKTS LQIHAKYPLG
     DVLIFLTGQD EIENMQAQLQ MYADDLTPTM PKMMICPLYA KLPPHLQQKV FQRTPPNFRK
     FILSTNVAET SITIPGVSYV IDTGFAKVKR FHSMAGVEEL RAEPISQSSA NQRTGRAGRE
     CPGKCWRLYS QETYNSLAKI TEPEIQRCSL SFAILHLLAT GVHDIFSFEF MDKPKLDDLK
     FALVHLALLG ALDSGSKINA LGRQMATLPL DPPLARCLLA SFDHRCASEM IDLIALLEHS
     DTLLVNTIST RELAQEARRK FIHRDGDHLV LLNILKAYQS TSENCQSQAK MKIEQKAWCK
     ENFINPKALS NVLESRKQLR DRCKRLGLDW SQSSRDPQES GEMISSVAEE DSSPILCSLL
     AGLATQLAIR QPDQSYINPI TKVHVKIHPS SSLYGKGVET FIYHELVHTS STYARMCSVM
     KPIWIQDQTT LFNSA
//
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