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Database: UniProt
Entry: M5EAZ6_MALS4
LinkDB: M5EAZ6_MALS4
Original site: M5EAZ6_MALS4 
ID   M5EAZ6_MALS4            Unreviewed;      1111 AA.
AC   M5EAZ6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Similar to S.cerevisiae protein RAD16 (Nucleotide excision repair (NER) protein) {ECO:0000313|EMBL:SHO77652.1};
GN   ORFNames=MSYG_1994 {ECO:0000313|EMBL:SHO77652.1};
OS   Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO77652.1, ECO:0000313|Proteomes:UP000186303};
RN   [1] {ECO:0000313|Proteomes:UP000186303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX   PubMed=28100699; DOI=10.1093/nar/gkx006;
RA   Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA   Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA   Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA   Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA   Lehtioe J.;
RT   "Proteogenomics produces comprehensive and highly accurate protein-coding
RT   gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL   Nucleic Acids Res. 45:2629-2643(2017).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; LT671823; SHO77652.1; -; Genomic_DNA.
DR   RefSeq; XP_018741241.1; XM_018884597.1.
DR   STRING; 1230383.M5EAZ6; -.
DR   GeneID; 30057616; -.
DR   KEGG; msym:MSY001_2731; -.
DR   VEuPathDB; FungiDB:MSYG_1994; -.
DR   HOGENOM; CLU_000315_2_7_1; -.
DR   OMA; YYVFHGP; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000186303; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186303}.
SQ   SEQUENCE   1111 AA;  125788 MW;  ACEFA9B9EB8E7F59 CRC64;
     MLGGTPNLAQ RGGAAPRTQA STIDLTLDDD DDEPILVETR VMPTSSSSSM PPARANQPSS
     SRATLSEDNN ADWSSFTPVF PKPKPWVCLG LIYPSVLCLY GVPPELRLDD PNDPPPVDPA
     WSHNAFWGEK GFRPVCIHAS LSTAQKSTPM SHFIKAQQRL DMVVSTLQPG HDGVQPTTLN
     EYGRLTDKFS KILAPFMQSR TVHCVSRAKL VNKLKARVFS QYIETLVFVR TEHVANVSEA
     LVQENILLEI PSEYRATDFP EAPPLHVPEM HRQEIEDVDD SPAALSPQRM NRFRSMIPAV
     TSREHLQEDS GKSSVEALYK VLQTHEPLTE TEPSPLIRTP LFSHQKQALT FLLGRERERQ
     WEELLQPDAP EHLSLWVSDK SHDNHIDVFR NMVSGVRRHS KPLLCRGAIL ADDMGLGKTL
     TTISLVASTY KEARDFGSSP LVQDTDDDEP MLIGDSRNRR SAEQARREEL RCRSRATLLV
     CPLTVIANWE TQIREHWRVD QQPSLYIYHG SGRVTDPYML ADHDVVLTTY STLGNEFSHQ
     NTWTAAAGRA DDDDLPESKR LRVEAPNTCQ RIEWFRIVLD EAHIIKEART WQAKAVCNLS
     ASRRLCLTGT PIQNRVDDLY ALVCFLRLDP FMDRAVWSRF CGDRRYLGLN SRGTGVDIDP
     ESLTRVQTIV KFLTLRRMKT DAKPDGTPLL VLPPKSTRIV TLDFREDELT KYKELHSQFR
     DEFNEYVSNG TVGQNYATIL HEILLLRMMC DHAELVDESM GQQKDSQEVA DLSETIRRYG
     LNVARALTLF RIWASSAMAI CSICTYDLSQ DDGDPTRVPV VTRCEHIVCS ACFQSHMGKP
     MWRSRGQGTC PCCHTELELA TDAVELSPET LRPSMPEEPT LEMIPRQVFH PDDPGTWPSS
     WSTKIRALIS DLLPFSRCNM YSELYDIKAP VLDHRVVTKA DNEFNVEVCT CDPLAKRPLP
     IKSVIFSQWT RMLQRVGHAL MHVGIQYRQL DGSMSRGERE AAMSDFRDEP RIEILLISLR
     AGGFGLNLVS GCRAYLLDPY WNPAVEQQGL DRIHRMGQAR PVIMTKFIMH QSIEEKLLVL
     QELKTELANS VGQPTEDRRQ ARTKELQLLL S
//
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