GenomeNet

Database: UniProt
Entry: W9Y9R1_9EURO
LinkDB: W9Y9R1_9EURO
Original site: W9Y9R1_9EURO 
ID   W9Y9R1_9EURO            Unreviewed;      1193 AA.
AC   W9Y9R1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=A1O1_06345 {ECO:0000313|EMBL:EXJ85976.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ85976.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ85976.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ85976.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia coronata CBS 617.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ85976.1}.
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; AMWN01000005; EXJ85976.1; -; Genomic_DNA.
DR   RefSeq; XP_007725414.1; XM_007727224.1.
DR   AlphaFoldDB; W9Y9R1; -.
DR   STRING; 1182541.W9Y9R1; -.
DR   GeneID; 19161213; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000019484; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17953; DEADc_DDX46; 1.
DR   CDD; cd22474; KH-I_PRP5_like; 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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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.
DR   PROSITE; PS51195; Q_MOTIF; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT   DOMAIN          555..583
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          586..764
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          791..941
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          76..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           555..583
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        76..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..385
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..988
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1193 AA;  131221 MW;  5AB8B8954C3A4F6E CRC64;
     MREVVGRMTE VIGGSTPDHG VLMYVAATVS PSLWINAYTL SAQRRYRDRR DRDRDGYRRR
     DRSIDRRYDS RRDDDYHYSR RDRSRDRRRS RDRDDRRRSK DRDTRSKRDD SRDKDRRPRD
     ESTESRKRKR ENSRARDTRR DSGGISREVS SKKTLQSYGA HHHLQTSKPR TPTHQTAEEQ
     KAARLAKLEQ WKKKQAEEQA RKQKELEASG GARSILNEID RKAELSPAVS SPQSPAANIS
     TTTAPEPTAP SSNSYSGKFD PKAIVKKAQH GPASAKVLGG DVPAPVLTNG HSSPKDQPNP
     ATNGSSTAKA LKAKGNLGKF GLGSKAATET DLSKSALAFE DDEGTKKTLL KLPDMQLETN
     GDSRAVNPDE VDGEDDVDMQ DEGTEEEAMA AARAAAEQRS RAERGEDTAM TDASAAVSTT
     DATDAQAEEE DVDPLDAFMQ DLQPQQNTKS FGQKSNAKSR QQEPEALFSD DDVDFTAIDD
     DNPDNILSLA NATAKKKKKD IPAVNHSKIN YEPFRRNFYS EPIEMAEMTE EEVAVLRMEL
     DNIKVRGVNV PKPVQKWAQC GLGVQVQEVI QRLGYEAPTS IQAQAIPAIM SGRDVIGVAK
     TGSGKTIAFL LPVFRHIKDQ RPLDPLDGPI GLILSPTREL ATQIHKECKP FLKALGLRAV
     CAYGGAPIKD QIADLKRGAE IVVCTPGRMI DLLAANGGRV TNLKRVTYVV LDEADRMFDM
     GFEPQVMKIL SNIRPDRQTV LFSATFPRQM EALARKTLNK PIEIIVGGRS VVAPEITQIV
     EVRDESTKFV RLLELLGKLY EDDKNEDDRA LIFVDRQESA DSLLRDLMKR GYPCMSIHGG
     KDQIDRDSTI ADFKAGVIPI LIATSVAARG LDVKQLKLVV NYDAPNHLED YVHRAGRTGR
     AGNTGTAVTF LTEEQDRYAV DIAKALRQSG QPVPESVQKL VDTFMEKVKA GKEKAAGSGF
     GGKGLERLDQ ERDAAKARER KTFKTGDEVE EEEEKEDSKD VKVGDDLFAK AASSVKASDA
     PAPSSSLPGV PKGIDLDGKI TVHRTEREAP SSGPASQMDK VAAAVGAINQ KLSKAGIMRS
     GVPIDNKGPD AGAFHATLEI NDFPQKARWA VTNRTNVAKI LESTGTSITT KGSFYPAGKE
     PGPGENPKLY ILVEGDTEVV VRDAMRELMR LLKEGTMSAA ESTERTGGRY SVV
//
DBGET integrated database retrieval system