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Database: UniProt
Entry: A8PVI7_MALGO
LinkDB: A8PVI7_MALGO
Original site: A8PVI7_MALGO 
ID   A8PVI7_MALGO            Unreviewed;      1564 AA.
AC   A8PVI7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MGL_0880 {ECO:0000313|EMBL:EDP44398.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44398.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP44398.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP44398.1}.
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DR   EMBL; AAYY01000003; EDP44398.1; -; Genomic_DNA.
DR   RefSeq; XP_001731612.1; XM_001731560.1.
DR   STRING; 425265.A8PVI7; -.
DR   GeneID; 5855918; -.
DR   KEGG; mgl:MGL_0880; -.
DR   VEuPathDB; FungiDB:MGL_0880; -.
DR   InParanoid; A8PVI7; -.
DR   OMA; ERISAYF; -.
DR   OrthoDB; 1095660at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_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   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46934; UBA-like; 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:UP000008837}.
FT   DOMAIN          744..914
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1027..1204
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..974
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1564 AA;  174669 MW;  263951E7B10CBF52 CRC64;
     MVKKKKPQLK SSVQRGFATT SVPKRETPTT NERTNDAIAS GATKQREAAE SSHPHSHPDG
     QMTAVATKMT DSHKSKGPTG GEDAFDPEAE ELQALQNIVQ QVYPKVEKET QRRGKTIQFQ
     QRFSKTLLPV SMDADVCAET LALTRDGREP ITKCEEATFL AEERGADGNK DNGDSDGRMI
     LQNMLGMSMP EESEAKALER ALTTWELLLS LGFSREQATL ALTYAPNLDI EECVAWLVAQ
     LDVRTYRTLS LNVDAPQEYV APKAASMDDS IPPMYDGYTF TRAEQSEMGS FADDAEKKKK
     KNDASKLVSA ASLDAETLDA IRRGTETVVT SLNALLDTDD ALLDVIEHPI EAWCTARIVA
     MQVDKDRSRR RKMLGGTPDD ELAQLVAEAE AQRQLDRLAA RTKDVMQQSE IQPQFHRTLA
     TQRFRERMRQ REAEEAEKMA AIQREEEAKR QRRSDIEQLD EQTSAGRGDE VANANRYEPS
     GTDTDADAHG DAKDNAPDPA DDDEAGALGD SAGLFEQPDE PGSSGATGDV SVRLRDIPAQ
     STQRSPRSLL TDVLKAVDPY AQHKFTLVSG KSAVRSQLQI QWNASGGRPP LVDTIKLTKE
     GCATRALADD YVATIALNCF GRERQVQRHL SKGFRDIWDE LEQMRMEQKH AFLRDEVLHV
     QHLLEHRNRA MRVPETEQAL KRDSRRAQPE SEPASTPSVR RSRTREAQPQ LAEMWAHRAS
     SKAYELMLRG RQDLPIYQAR DTILQSVATS QVVVLSGETG CGKSTQLPAY LMEDCLARGE
     PCKIYVTEPR RISAISLAER VSQEMGEAPR SVGSSESLVG YAIRLESQIG ANARLIYATT
     GIVLRMLESS VLDDVTHIIV DEVHERSIES DFLLIVLKTL MHERPDLKIV LMSATLDAER
     ISAYFGGCPT LAVPGRTFPV DVHYLEDVLE LCDDYTLDLN SPYARQTEKL NKVEVQEDVD
     GDLVDGEEDD GDSHDNEDKA ASERKKLDDA GAVSQVNGTT NGPTPRYSAK TIDTLLHLNE
     HKINYELLTA LLERICTEPK YASFSRAILV FLPGMGEIRE CLRHLTELRR FQTECQVHVL
     HSSVATEEQS AAFLPPPEGQ RKIVLATNIA ETGITIPDIT CVVDSGRHRE MRYDEKRKIS
     RLVDCFIARS NAKQRRGRAG RVQHGICFHL FTRKRHDDYM DPHPVPEMLR LSLQELALQL
     KVMPLRIGTS IENALAQALD PPLAVNVQRA VASLVEVEAL TPNEDITPLG RHLCHMPLDV
     HLAKFLLVSV LLGCVDAALS IAAVLNAKSP FLKSMGRETG RGRSAFQTHD SDFMAFAQMF
     HAWRAAVGRH QGQSFCTAHS LSADVLYQIE ELRQQYFAYL VDTGFVRVEA SVRNDLARRR
     ARHGRPKLMS IPEHLDVYGQ SAPVVTLALV TAMYPKLLQV DENTQQMRTL LNNQPALVHP
     SSVNARRALG TTSTHFVLYH AIVYSFRLYA WETAVVDDRM VLLIGGEAEF KHTSRSMYID
     HNRVRMTTYD APSLVALRVL RTQLRELFQA SFRSPGRPWT RTQHRMMELV LKSLGVPVKP
     PLST
//
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