GenomeNet

Database: UniProt
Entry: U7PTY9_SPOS1
LinkDB: U7PTY9_SPOS1
Original site: U7PTY9_SPOS1 
ID   U7PTY9_SPOS1            Unreviewed;       627 AA.
AC   U7PTY9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=HMPREF1624_05165 {ECO:0000313|EMBL:ERS98381.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS98381.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI440846; ERS98381.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PTY9; -.
DR   STRING; 1391915.U7PTY9; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_1_5_1; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000018087; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
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   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 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, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   DOMAIN          193..393
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          432..597
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  68522 MW;  FAE5AD1E606F3A65 CRC64;
     MSIKKHRPVD EEDVDTPAAP LAKKARVAAN GDAANGDEAE RRQLKKEKKD KKRKEKKEKR
     EKEGKEGKEG KDDQEAKKEK KDKKKEKKEK KLKEKGEATE GTAESTTATN GATPSSGSYT
     QTAALTAVPE ADVQAYLKKE QVAVYDPVVS KTAPASERLR PILEFSQLPA TALTKKGPFA
     AYKNPTPIQA ASWPYTLGGR DLVGIAETGS GKTMAFALPC VEALRSLPKP AAVEAKKLPN
     RSKLNNKWDA RGNLAQALAV IVSPTRELAM QTHQAIEPLA ALAGLTAVCL YGGASKDEQR
     VLLRQEGGVD IVVATPGRLK DFINDEAVSL AHVQFAVLDE ADRMLDTGFE EDIKFILGQC
     PERAARQTLM FTATWPTSVR GLADGFMKDP IKITVGSRTR AGALDGEDGA EGGDGPRDRN
     NTGAVELQAN ARITQTVEVI DQREKERRCL NIIKQEQRGK AKNDRILVFC LYKKEAVRVE
     NFLQGQGVRV CSIHGDLRQE QRTRSLEAFK AGTTPVLVAT DVAARGLDIP EVKLVINVTF
     PLTIEDYVHR IGRTGRAGKD GRAITFFTEH DKTHSGSLIN VLKGANQEVP EDLLKFGTTV
     KKKTHGTYGA FFKDVDMSQK GTKITFD
//
DBGET integrated database retrieval system