ID H6QQ22_PUCGT Unreviewed; 1427 AA.
AC H6QQ22;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ATP-dependent RNA helicase A {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGTG_20968 {ECO:0000313|EMBL:EHS64505.1};
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:EHS64505.1, ECO:0000313|Proteomes:UP000008783};
RN [1] {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).
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DR EMBL; DS178268; EHS64505.1; -; Genomic_DNA.
DR RefSeq; XP_003890419.1; XM_003890370.1.
DR STRING; 418459.H6QQ22; -.
DR EnsemblFungi; EHS64505; EHS64505; PGTG_20968.
DR GeneID; 13542649; -.
DR KEGG; pgr:PGTG_20968; -.
DR VEuPathDB; FungiDB:PGTG_20968; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_1_1; -.
DR InParanoid; H6QQ22; -.
DR OrthoDB; 1095660at2759; -.
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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd00048; DSRM_SF; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014720; dsRBD_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:SF203; -; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 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 416..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 676..853
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 157655 MW; 5E29D1EF7D088DAC CRC64;
MADISSSWRS NSNRNTALYP TADHSHHNPY SEINNQYYSQ QAHPPRASNG KGRGRGKAKR
SGGPQRPNFS HLPHLGYPIY NSQEIRKFWT ANLPPRPEWS QNPKGILNNF CQHLTHPLPK
YHSQQVILPG FTQPLFRATV HLEIAPDIVG IGDDLSKKEA EKIAALSVCF QLGMKNMFDE
NNLPVSSLNA PPDGKPRNLM PDGTQLTLDQ AKAYMSFYCR KFNFGSPEIQ YENGKKGRPT
WIATIFVGGR KIGLGHAVNK KDSLNEAYID TVVYLGECDP DLWVEFRQSA ESQEAAAGGT
IPAVVFKLSN QTEQDLRQIV YSSMDCELYR RAKTLLERTR GSASAPHQAN QGTANNPSRK
NQTNNTSNSR QSALKEKSSA LRDRLDAYQT NTSPEVVKLR EQRQSLPVTA HSSVVSSALA
SNPITILMAA TGSGKTTQVP QLILDEATMK GEGAKCNIIC TQPRRIAAIS VAQRVAAERN
EKLSESVGYQ VRFESKPPTP DGSILFCTTG IFLRRLQNDM DSATGGFLDS ITHIVVDEVH
ERDIETDLLL FCLRRVLKDR KEKGKSEIKV LLMSATVDPT LFEQYFSDGN GGKPAPVISI
PGRSFPVEKH YLEEVHRDLR QLNLPTARGG WVWGDPKVQK YTQRELQEPL ALDPVTGKSL
RDSDDLEMPF ALIALVVAWV LSKSSEGHVL VFLPGWEEIK GVQTILTDPR QFPLLNLNFN
DSSKFEVHVL HSAIPVADQQ LVFSPPPKGV RRVILSTNIA ETSVTIPDVV FVVDTGKIKE
KRFDPERHLS SLITAWVGTS NLNQRAGRAG RHRSGDYYGL LSKRRYDALN IHSTVEMKRT
DLSNLVMHVK ALNFPNMEAE DVLAQTIEPP ERERVSAAMS HLQSIGALDR HKDLTALGRV
LLQLPVEAQI GKLLLLGSFF KCLEPALNLA AILTNRDPFL SPPAAKAEAD RVKSSWAPLE
FRSDPLASLA AFKAWSNLHA AGDNYKTNKF TNENFLSRPA LFQIAQVKTH LLASLRRAGV
LAISGGGGQS DNHYSRRNDI PPHLNKNSDS LPLAAALIAV AVAPNFAVRK SARVFATDKD
RTCIIHASSV NSYKKQAAAG DDIPLQNERQ LFAFGEKSLL PQRPGEKGKE QMSLRATTRL
DPLGYMLFGA RQLQPYPSGL RCDGWLPITG NAGALDDVER LKHVLDASLL RVFDGLLAQT
IENNPRLPKR RARVVLPPPK RISAAAKKAQ EADEEESVDS EFEVDEEEDQ DEVVPVQFGK
LTHGEIQDLQ RLTEEVVSLL NKYSEERLAT DVNTSRAPSR PDSRATNRPL INRLQPMGYG
SEGGGVHGGN SSAGPSRPGS RLTNQIEPSN THPAQQSSWN HPGPAIQHGV PSKLPPGVGY
MNWSNGVSSF PPPPPPASSQ GGTWQQQQQH PLQQRNPHPS SSSARWR
//
