ID E3K433_PUCGT Unreviewed; 1444 AA.
AC E3K433;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PGTG_04791 {ECO:0000313|EMBL:EFP78835.2};
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:EFP78835.2, 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 -!- 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};
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DR EMBL; DS178271; EFP78835.2; -; Genomic_DNA.
DR RefSeq; XP_003323254.2; XM_003323206.2.
DR STRING; 418459.E3K433; -.
DR EnsemblFungi; EFP78835; EFP78835; PGTG_04791.
DR GeneID; 10536937; -.
DR KEGG; pgr:PGTG_04791; -.
DR VEuPathDB; FungiDB:PGTG_04791; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_0_4_1; -.
DR InParanoid; E3K433; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA 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:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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 InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 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 162..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 382..577
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 161896 MW; 5B7FDFB0048DA6EA CRC64;
MDYSPARDGL QERYPLFKPP SPSQSESISD YFDDGLDEGS LNNLVDNIDR HAQYPSIQAQ
NLPFESNDQQ SDRYYSPVPQ MSRNSFNRNS STEFPDQYES QSVYPDNPAV DSTYQDNHYQ
PVGPHRPRVS GPNLIPVTAL PEPYTDFFSF SHFNSVQSEC FPTVYGTNHN VLTNAPTGSG
KTVIFELAIL RMLEYNQVSK GVYMAPTKSL CAERFRDWST RFGSLGVKCV ELTGDSENAG
LADAKLANLI ITTPEKWDSM TRRWFEFSKL LNKIRLVCID EVHMLNEERG SVLEVIVARM
KTLGTNIRLI ALSATVPNIS DVAEWLGDGG VADQNEMALT GQAPAKTFIF GEEHRPVKLS
KFVYGYTPCT NNSEMFNCLE SRLMDHITTH SSGRPTLVFC GTRKSSLQAA ETLSKSYQKM
SSQGEKLPWE APKSAGTFSD KKLTELGAQG IGVHHAGLDQ SDRRQIESLF TLNKISVLCT
TSTLSVGVNL PARCVIIRGT KTYRGGTSSR DGFEDYSELD LIQMMGRAGR PQFDDEGVAV
VMTSQNDKMR IEKLVKSETM LESCLHLNLT EHINSEIYMG TIISRSSAID WLENSFLSVR
IKKNPKHYSI SDDQVAPDQQ LGKFAGAALD LLLEDGLIEE DEDQVIRPTE LGEIMSKFCL
RHKTFLGLAR MKSSATMRNI LEIVSGAEEY CTLRLRAGEG VAYKALNSHP EMKCPIPGKI
TQTWQKAVLG GIPLAEVKVE NANPLMEVNI IWQHLPRICK CLVALSISRH DAAIKSCLEF
LRSVTAKAWD DSPWVLRQLD SIGEKSVKRF VDAGIATIDK LQNTSNHRIE MILDRNPPFG
TRIVRQARSM PKFFCTMETI SETVVPEGVQ VCVEITVGLS DTGETPVWKW KNYILMATVL
VMTNDQEWIE FRTIQVKLLR ETKQFNVECI LVKPSQTIVT QVACTQLAGI GVSSRWKPRT
SREHYPKPKT ITDDQAASIE VLQGLNTKDL AASSTESECE FLEKPPKSMS KSSTQIARPV
HKADKVCPKS QAPNGTAEPK RPVTEVRERL KNGRYKCAHR CKGACHHVCC RDGVSKPPKI
REANKISLAN STDSQYSGSQ KSLPLNPIRT TNITRTPEDW QKIRQAVPGS SFHANQPKLS
GRIKPIKKIP EAIQVDRHDE LPSLEELQEM STIETEKTRP SKGIGGGNDR KAEVRSQHGN
EKELDPVPKT AKRPKEVVGI EKFRNMKKIV EDFDERGIFH QQKEIPIPPP VNLPDVAVVE
DTEPRDSKSL SLSPDISFPP CNNSHNDEER PQASEGEDET DELDEDWDIK IFESYLAPEE
SRKALEAKES AVTKRQIDQS YGNHSGPTPK KQKLTTTEYF KSLSPPDNEE NWPQYPSRDN
SKDPRENADD QSPRQPTFTR EGEAQAESEK APEDDEYDEL DSDDSMTARM DEVLAWAESH
VIKE
//
