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Database: UniProt
Entry: E3L6A3_PUCGT
LinkDB: E3L6A3_PUCGT
Original site: E3L6A3_PUCGT 
ID   E3L6A3_PUCGT            Unreviewed;       632 AA.
AC   E3L6A3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=ATP-dependent DNA helicase sgs1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PGTG_18168 {ECO:0000313|EMBL:EFP92078.2};
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:EFP92078.2, 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   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; DS178357; EFP92078.2; -; Genomic_DNA.
DR   RefSeq; XP_003336497.2; XM_003336449.2.
DR   AlphaFoldDB; E3L6A3; -.
DR   STRING; 418459.E3L6A3; -.
DR   EnsemblFungi; EFP92078; EFP92078; PGTG_18168.
DR   GeneID; 10532035; -.
DR   KEGG; pgr:PGTG_18168; -.
DR   VEuPathDB; FungiDB:PGTG_18168; -.
DR   HOGENOM; CLU_011478_1_1_1; -.
DR   InParanoid; E3L6A3; -.
DR   OrthoDB; 1506797at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   SMART; SM00487; DEXDc; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          62..256
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          288..445
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   632 AA;  71218 MW;  A1FEB5A1226BDE28 CRC64;
     MNRASKNPPP TIKPPPARWA SLGITVLKKI AEKKDDALRR EILEISRSLY GQDAKTLQID
     AVVNLVRGRN TFLLAGTGYG KSRIPELYFR TLPISEKPVI IVLNPLDSLG DNQVLEKKAA
     KFTAINLTSL TFNKDEAELI ANGFYNFVYL SPEIFLNSKM WDRVYFSDMF QRRLGLVVLD
     EAHMVYEWGI VEKTRGRKRS SALGRHEDRG IFRPSYGNLG GHLMTRNNMP MLLMSATCRP
     VAIEAIKTSL KLSDHTLRML NGELTRPGIR FIRVTMDYSL SSCEDLLDLY ARKTTTPDEK
     VVPTIIYSGS RHRTMKVLDV LDRARGSADS VNNSESTFAR RFHSITGDLC KIDVADDFAA
     GKFPIVSATM ALGLGQNWSR VRSVIHMGRG DPAAICQMLG RCGRDGRPGV AIMFVEKTRI
     GGKNRVDQIL DGVEQSDDDR MDGLAITPVC LRIAFSLDTK LGYIPMSIKD QGYQNEKSRE
     ERLGFAQCRC SNCMPMEANT FIENMKLMTV DNIDRMITTD LNAYETGALV PKHPKLKIQR
     PWMSNKRALA DPEDLRNFKR QMRETVDELH QNEHGDNTFF TPSQLFQDKK IDLIAHHADK
     LLTLKDIREK AHINAKEDSN KLASGGRNPS TS
//
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