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Database: UniProt
Entry: E3KQM4_PUCGT
LinkDB: E3KQM4_PUCGT
Original site: E3KQM4_PUCGT 
ID   E3KQM4_PUCGT            Unreviewed;      1306 AA.
AC   E3KQM4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=PGTG_12981 {ECO:0000313|EMBL:EFP86599.2};
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:EFP86599.2, 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|RuleBase:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
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DR   EMBL; DS178301; EFP86599.2; -; Genomic_DNA.
DR   RefSeq; XP_003331018.2; XM_003330970.2.
DR   STRING; 418459.E3KQM4; -.
DR   EnsemblFungi; EFP86599; EFP86599; PGTG_12981.
DR   GeneID; 10540699; -.
DR   KEGG; pgr:PGTG_12981; -.
DR   VEuPathDB; FungiDB:PGTG_12981; -.
DR   HOGENOM; CLU_261088_0_0_1; -.
DR   InParanoid; E3KQM4; -.
DR   OrthoDB; 1611579at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   PANTHER; PTHR10492:SF57; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR10492; UNCHARACTERIZED; 1.
DR   Pfam; PF05970; PIF1; 2.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          1161..1204
FT                   /note="DNA helicase Pif1-like 2B"
FT                   /evidence="ECO:0000259|Pfam:PF21530"
FT   REGION          100..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1306 AA;  143093 MW;  E979A5DDA60B66F8 CRC64;
     MADNGGGSSS DAMVKIKPQN EDLAFNGSNV KRFLSEYQLA ARLDGASEKD MAQQLGFFIA
     KDKLLDVVET LEGYEPPDWP KLKASMIAYW GNVDTTKFSL PDPVPSDQSL EEENPQNLER
     GLPLGSHNDL LVEEALESDS NFVDLDVGPE LFDKSSKQDR NESIKTREPA WHPTNTSLYF
     TAASAIEYPL ASRINKSNPS RRQHENLKSS TVLSVSLPPV KDSTLPVPDS DQEDMDDNPE
     LFEQSTEDPS PAEVTAARLI LALNPVASPI NNHLSTEISE NLSSASASAA TKDKEKFLVD
     QKGHNYFLPS GAWIPFDPVR PIRSVVTAFQ ASSRSAPPFP APYRISCGAL QPWYPTTKPI
     PCADPPVSES YHCHLIRKSP NIKSSQPKVL SSDPPSPKCL AKFVKEANSV LKKIINLMVP
     GFSASSLDNV HLPKSQIPRR TKARKVIPRR HNGVKVSSLQ YAPPGLDATK IVKTLSRATL
     VSNGQPSALD SPGVPDPTSS ETLRDEVKLS SDPPLCSVPD LDPIGQLRPT SERMVSFPIA
     LRDEVKLSSD HSLHSVPNLD PIGQLRPTSE RLVPSSIALQ NEVKLSSDPS LCSVPDLDPI
     GQLRPTAESL VSSSIRLHKE ATLNSQVQES VFSSQASSDP NNHMSSLSHN YQSHPSGVPK
     SSITPEVHQS QSSQPLSNSV DPLSSSSPIR LRNEDKPASV PIPNPLRNET KQTSESSNVE
     YPDPVSSDGV QASGQVENDL CNEGELGLLH FDEEEGWMIE VFPRGGKVDQ NPPSRPQGLL
     EEFIEVLSDN LIYKLQNTYN IRNPSLEQRT SLCYYLIKQI LAENGKSLAD VGLRPIAADD
     RLWWYFDTVS AREETMRITD HTNRFLEMSA RLNQKQSAIA DAVIGLTSAG EAGLIYVDGP
     GGCGKTFLLN TLIHYFNASE IPVITVASSG VASLMLINGM TAHSRFKIPL NVKYAVEAVD
     QAFRSLMDNE QPFGGKIVIF GGDFRQTLPV VPGGSVLDQG RCCMISSAIW NDVFYFQLTQ
     NLRLRASGDD QSARSNLLRP TGFAEWLLSV GNGSGQTDFT ADIDIAFGWV YRHSDARVVA
     ERAIVKTYGD MAVALNDPEA GRLNAYFGNR LILAPLNSDV NRINAICSSR LPGEVFVSHS
     INQMRNEEDG EDSDEAIPEE VLRTFSIPGF PEADIELKVG MPVILLRNLD LKRGLSNGTR
     LLVLAIRPDA LRCRILTGSC TGAEIAIPRI RHGPKYSFAS TRYLFSSTCW ECTSTRPRVA
     GAKVQVTGLT TNPRSHWSHA HRQTHPSNRE VLFIAPSNPD QPHPPR
//
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