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Database: UniProt
Entry: A5DM35_PICGU
LinkDB: A5DM35_PICGU
Original site: A5DM35_PICGU 
ID   A5DM35_PICGU            Unreviewed;      1426 AA.
AC   A5DM35;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PGUG_04336 {ECO:0000313|EMBL:EDK40238.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40238.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK40238.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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DR   EMBL; CH408159; EDK40238.2; -; Genomic_DNA.
DR   RefSeq; XP_001483607.1; XM_001483557.1.
DR   STRING; 294746.A5DM35; -.
DR   GeneID; 5125591; -.
DR   KEGG; pgu:PGUG_04336; -.
DR   eggNOG; KOG0951; Eukaryota.
DR   HOGENOM; CLU_000335_1_0_1; -.
DR   InParanoid; A5DM35; -.
DR   OMA; QTEIQYY; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18019; DEXHc_Brr2_1; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; 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; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT   DOMAIN          457..641
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          676..886
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1426 AA;  162243 MW;  EF7F6AD75A54C00E CRC64;
     MSYNQYKYEE MSNMVLKPGR RPREEISDAP SSLSGRISVK EMGSRVERVK PTSENDQERP
     SKNPSTTKSD GYAPEVSTEV SYYPTTAENG HIFELLMTSV NTILPDSSHE VILSAADAVL
     DICKQQDVNN KQKQSEIEAL LETKLDSNAF DEILKLCNRI TDYDAREENE ETEENLDGVP
     IVFDEEDEED ENPQDSEEED DKIVGPSIEP NDQDSSLVGS NDITVKTETT QSASESNIIP
     LHEIDQYYLQ RRLAFIYGDE NASETQTMAE KMNKLLQNAD LSTRDLENEL MEILDYDHFD
     LVTFCLENRW RLVYKMKLLD GVDETKVYDE MRSLNLHGLV DEFQGVRQSS KRRLSDSETS
     VKKQKKISTK RQPREVDLSA LAFDQGSHMI STNRVKLPPG SYQQKKKSYD IISIPAPTPA
     EDNDPLISIS ELPSWAQEVF PSSETTNLNR IQSKIYPSAF KTDENLLLCA PTGAGKTNVA
     MLTILRTLEH YRKEDGRFDL GEFKIVYVAP LKALVQEQKR EFERRLTPTF GITVNELTGD
     SSLSAQQISE TQIIVTTPEK WDVITRKGSE VPHVSLTRLV IIDEIHLLHD DRGPVLESII
     ARTQRQMESS GEPIRLVGLS ATLPNYKDVA KFLRVDFEKG LFYFDATYRP CPLEQHFIGI
     KEKKAIKKVQ AMNEACYDKM IESLESKHQI IIFVHSRKDT YKTAVWLRDK LVENEKLNLV
     QTTAGSKEIL RQEAEAVRNQ NLAEVIGGGF GMHHAGLNRD ERSLVEDLFA QGHIRVLVST
     ATLAWGVNLP AHTVVIKGTE TYSPELGSWV QLSPQDILQM LGRAGRPRYD KSGEGVIITS
     SDDIQYYLAI LNQQLPIESQ MMSKLVDIIN AEVVLGSVTT RQQVVEWLSY TYLYIRMLRA
     PALYRVGADY ADDKLLSDKR EDLSHSALQI LHRHKMVQYD MESGAIKSTE LGKIASHFYI
     GYETISAYNN NLKSWSTIVD VFRIFCMSGE FRLIPIRQEE KLEVTKLAQK CPIPIKEAAT
     EPIAKVNVLL QTYISRLSLD GFALVADMVY ITQSAGRLFR ALHEIALKKK WSAIARTTLD
     VCKMVERRMW LVNSPLRQFG ELASPQIIRA AEGSHLPWNS YFDLEASELA EAIAFKGNSQ
     KVHQLLQQFP RNKMDYLLQP ITSKMIRVQF EIVPNFNWNV NLHGNSQRFL LLIEDCDGET
     ILFSDNFTVY RRNAQKPHII EAAVPFMDPE QPQYFASVIS ESWINCETRI PLMLNNIQVP
     KKGSSFTELL DLHSVETSEL KNEAFSKCFD FRYFNRFQSQ AFNALYWTSH NVLVGMSKNN
     GKTVCAELAV LAHWRAGGGR IVYLNPNLEK LKRVGKSWSK RFHGLTDPPK EINCLSGDPT
     VDLALLSSSH LVLATPDQWD RISRRWKQRR AIQSVDLYVA DRCTFG
//
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