GenomeNet

Database: UniProt
Entry: M9LVR6_PSEA3
LinkDB: M9LVR6_PSEA3
Original site: M9LVR6_PSEA3 
ID   M9LVR6_PSEA3            Unreviewed;      1319 AA.
AC   M9LVR6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Helicase-like transcription factor HLTF {ECO:0000313|EMBL:GAC74054.1};
GN   ORFNames=PANT_9d00405 {ECO:0000313|EMBL:GAC74054.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC74054.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; DF196775; GAC74054.1; -; Genomic_DNA.
DR   STRING; 1151754.M9LVR6; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 2.
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; IPR014905; HIRAN.
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:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 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   Helicase {ECO:0000313|EMBL:GAC74054.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          616..851
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1064..1110
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1152..1311
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1319 AA;  144496 MW;  575B14DA41548993 CRC64;
     MTSQSSLEVQ SQPSRDFFAS SPSATPSSPR KPAQRQLEPP ASTRQPQSEE AAAELDATED
     DFSIVGSTSA QNDQPSRRQQ PRRAAADNAK PLFLADEDED LDAWGGEDDE QVAAASSDFF
     STQIDTQAKS AQRQKVKSDD EEFVPSAPSH ANGDRSSSPS EPQRKRATET AYAATKNGNA
     KRLRSSSSSP APEASRKRSP SPDPRLRHDA FDRRFLGTFV LSAWSLSKGS SYVKPGDPVR
     IFRPRKKPLP AETTSKASKL TNGGVKKTKQ ATLNFGGAAS SPTSFFASKQ KSKDKQDFIV
     RFSNMRGFEV GRLPLEVATW MSKLIDAGIA DFEGVVVDCP ASLTVGCDIL LQVKAYIRFD
     AFFLSLTALA NGGFDEQNDG LRPETAESEI EKSLRERKIS LVRMFRVCDL KPSLSNSILK
     AHKAVDDFSS DAMLDQYGGD VAASAQAVAA EPASSPSAPI EVDSSSDEAA AAEGGIATQL
     QEAQRQTDGD ADVDENDGTE LNLNQLDEVY RKAQANDAHL PEVEPPDTFL LTLRPYQKQA
     LGWMKNMEKA PGPSSQQDEA SQANAGERNL SLHPLWEEYE FPLDYDHPEA NERLVLSPTR
     MFYFNPYTGD LSLDFQRASK GSRGGILADE MGLGKTIMVT SLLHANRRAE EGEESSDEEV
     GDGEDGWAAS GKRRGAAKQT SLASAFAASA SSGDARRALL RASVAKGKAS LVVAPMSLIG
     QWRDEIMRSS APGSLTPMLY YADSKADLLA QLESGKVNVV ITSYGTLVTE YRRFLDGGGA
     ANRHLSSTAP LYCIDWLRVI LDEAHNIKNR STMNARACCD LVSRRRWALT GTPIINRLTD
     LFSLLKFLRV EPWGDFSFFN SFVCKPFQAK STKALDVVQV ILESVLLRRE KRMKDKDGRP
     IVELPPKTIE VRELEFSPIE RRIYDNVYRR AFMQYATLKA NGTVTRNFSV IFSVLMRLRQ
     AVCHPALVLQ ARKGKTKGGD TDAAASEEVG GAEAGVDEED AAGFGDGGDG DATPGMEDLR
     ELVAQFQSAE EGEGEAESGG YSRAMVDRLL TNAGGDAAAM ESECAICFED PQIAPCYLPR
     CMHSACKACL LGYLQQCINR GEEPACPTCR TGPVAASDLI EAIRTRPPAS PDDRGGMIYV
     RNNLLTSTKV SALISHLNQL RAEGSFKGVI FSQFTSFLDV IQPVLARYHF RFLRLDGTTP
     QKQREKLLVE FQSPAREGEV VLFLISLKAG GVGLNLTAAT KIWLLDFWWN SSIEHQAIDR
     IHRLGQTKPV NVYRYLVKDS IENRILQIQK RKDSLIHHAL NKDPKQTDTV GDLDILFAE
//
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