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Database: UniProt
Entry: G3AEW1_SPAPN
LinkDB: G3AEW1_SPAPN
Original site: G3AEW1_SPAPN 
ID   G3AEW1_SPAPN            Unreviewed;      2024 AA.
AC   G3AEW1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SPAPADRAFT_131497 {ECO:0000313|EMBL:EGW35791.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW35791.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR   EMBL; GL996499; EGW35791.1; -; Genomic_DNA.
DR   RefSeq; XP_007373203.1; XM_007373141.1.
DR   STRING; 619300.G3AEW1; -.
DR   GeneID; 18869581; -.
DR   KEGG; spaa:SPAPADRAFT_131497; -.
DR   eggNOG; KOG0951; Eukaryota.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   InParanoid; G3AEW1; -.
DR   OMA; QTEIQYY; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
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; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
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:UP000000709}.
FT   DOMAIN          401..582
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          592..823
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1242..1413
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2024 AA;  230441 MW;  FF82200942444A38 CRC64;
     MANKVIRQPR KGTSEQEVPA SSMAGRINAK DMGSNYKPEH KTVTKTTKQE ENSSLPNYQL
     FEVFMTKIRT YLPDSSHEVI RSATELAVEY LSKPDLSVVK KREELEELLS AKVDDVDLNV
     LINLTDKMNE LNSVKQDDNE NEYIAVDFDS SDEEQGQADV EVEVEEDEEQ PEGEQEVIEL
     PEVSKDPEVV NIAWLEQEVL KASKTHELST SAELLLSDTI RLLSDVELTV NELDNSLNEV
     FEYECSDLIV KCIENRWRIV FTKKLSEATS EETRQEIYQE MEALHLEQLA SELEDKKRSA
     FDDEAEVTSV KRVKQGKRIP QRISLDKIQF STSVEGTKVI LPKGSFQQNK KSYDIITVPP
     VEQAPQTEDL LPINSLPDWA RDAFPSNETT TFNRIQSKIF PQAFETDNNL LICAPTGAGK
     TNVAMLTILR TISNFRTEAG RILLKQFKII YIAPLKALVQ EQMREFQRRL TSYGLVVNEL
     TGDSTLSKRQ ILETQIIVTT PEKWDIITRK DPSYISLTRL IIIDEIHLLH DERGPALENI
     VGRTLRKSET TGNQVRLVGL SATLPNYADV AKFIQVPEEG LFYFDASFRP CPLQQEFVGI
     KERSAIKKLN AMNEACFDRT LNSLERGHQL IIFVHSRKET YTTAKYLMDK MASSEVNMVD
     TLGVKEILKQ EGESMSNKHL KEIIPNGFGI HHAGLSRNDR NVVEDLFASG HLRVLVSTAT
     LAWGVNLPAH TVIIKGTETY SPEIGTWVQL SPQDILQMLG RAGRPRYDKN GEGIIITSQD
     EIQYYLAILN QQLPIESKLI SKLVDSVNSE VVSGSITTLE EGIEWLSYTY FFVRMLHSPA
     LYGIEADYDF KGDPTLHNRR ADLIYTALAI LHENKLVMFE SETGLVKSTE LGKISSYYYI
     NYETINLYGK MLKPWYNEID ILRVFSNSGE FKYVPVRQEE RLEVSKLMEK CPIPIKEQPH
     EAVAKINILL QTYISRLALE GYALISDMIY ITQSAGRLLR AIYEISLLKK WSGLSKIVLD
     LCKMVDKRIW LNNSPLRQFG SLVPDQIIRA TEMSHLPWNR YFQLTVEELA EAINLKGNAK
     VASEFIQAFP RISIQYFVQP ISSKFLRVQI EAVPEWSWMS VHGSQEMFMV FLEDCNGNQL
     LHHEEFVVKQ QNINKVHVVE FIVPVSEPLI PNFVVSFISN KWVNCNWKVP IMLTNVEVPS
     LSSYYLDNSD VQLVSTKDLK KQEFIDLFPF TFFNKVQSAT FDVVYHTNEN VFIGSSKGDG
     KTVCAELAIL NHWRQNKGRV VYINPSTEII DDNLKKWSNS FDVFEKSVNK LTGTLRQDIA
     ILNESHLVLA TPEQFANLSK RWKTKKSFKS IDLLILDDIH FIGSLPTYEI LVSRIRMLTS
     QWDNMLRIVA LASPVANCRD LCDWIGVGKS NVFNFPPQSR QNSISEIKLS PEGSVVPIVK
     IYKELKRLNV GLRKSVIFVP TRVKALELAR QLLDYMAGSH DWRRVDLLKL EKYIEKVEDN
     TLRELLGRGI AVYFENMSRV DKLIVEKLFE SNSIGILIAT KNTCKYAPHG HNLLVVGTQT
     YDGYEHRNVD CNSNEIFEMV GCCQDDLANE GKVHIYTENK TIEFYGSLLN DGLIVESLLL
     SSISEFFMGA ISNGVVRSKQ DCIDLLTFSY FYRRLVKNPG FYELKNATSL GVSEYLSELI
     ENAIEELEKN EFVEIEQDEE EETILPLNKT IIASHYSISY ETMKLFGSLT SKSKLKDILL
     IITSASEFES IPVREEDGNV LSRLGQKVPI KLNGEHDIES PLYKSFILLQ SHISRIEVPA
     ELAQDRNTVV TKVLDILNAC IDCLSGEGHL NALLAMDLSQ MIIQAVWSTG AGSALRQIPY
     FDDAILARCE KHNVETVYDI MSLEDEERDE VLQLEGDRLN SVANFVNQYP NIEISYEMDT
     ATPCVANEPK EITIKIERDE EMESLQVVCD KYPSAREEGW WLVIGDAQLR QLYAIKRVSL
     GLESQNFTLE FTVPTKGKAN LTVWSICDSY IDADKEINFD IEVV
//
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