ID B6QA99_TALMQ Unreviewed; 1177 AA.
AC B6QA99;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=SWI/SNF family DNA-dependent ATPase Ris1, putative {ECO:0000313|EMBL:EEA25226.1};
GN ORFNames=PMAA_063450 {ECO:0000313|EMBL:EEA25226.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25226.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; DS995900; EEA25226.1; -; Genomic_DNA.
DR RefSeq; XP_002145773.1; XM_002145737.1.
DR AlphaFoldDB; B6QA99; -.
DR STRING; 441960.B6QA99; -.
DR VEuPathDB; FungiDB:PMAA_063450; -.
DR HOGENOM; CLU_000315_2_0_1; -.
DR OrthoDB; 200191at2759; -.
DR PhylomeDB; B6QA99; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 461..651
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..861
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1005..1166
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 53..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..933
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..973
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 133178 MW; 0E4BE2E5483B826B CRC64;
MTSSFDEMSI EDIIDELDLN KALLESLIES RPDDVEEREE LEATVMDLER KLAGRRGVPY
NPPAAQQPQS SSRAAYQYDG AGDSPQGSGV TNDHDDDGFT ASLPHHDTPH RKRNLDPSDI
GDYSGSPVSK RARSRHTRSP VPSAPYGSSV GRNNYDPLDD YFQDDDIDFR EGQYEAEKWL
EERRAQELKD EEFARRLQES FEDEFSYVPS KQTQPSQPPK ADSYNPYSSS STNPLKPMLN
SQSPFMQKPT LPSSATREQP AFGMTGFGHP ASYQYPSQAP SSFGFQPTKY PTLGASSNQQ
VIDSSDEDED FMEIGASDFY GNDSHFYGNN YRLPIFTRKK DNISMGTGVV RYGSEMPNRN
TSLGYLPKGR SPKPWMKVEN DLPVAAPWLN IELVDNSLNF FDRELMLCRD ETVDSKQANQ
ELKSLLENLR PDFDISREAT PEQLNFPLFE HQKLGLAWMK AMEEGQNKGG ILADDMGLGK
TVQALSLVVA RPSTDPSRKT TLIIAPVALM QQWKREIDRL IKPEHKLSVF ILHGEKRKTA
FDKLKRFDVV LTTFGSMGTE LKKREQFDEM RRFAQSNANL IAEARGLPLL GPDSTWYRVI
IDEAQCIKNR NTKAALACYS LNATYRWCMS GTPMMNGVHE LHSLLRFLRI GPYNSLPLFN
STFTRPLKGS NKEDQTRALT QLRVVLKAIL LRRTKFSKLD GKPLIHLPPR TTEKIHAVFS
EDEQQLYDAL ESKTQIQFNK YLKANSVGKN YSNILVLLLR LRQACCHPHL IRDLSVDISA
VTEQADFAEN AKQFSPDVVR RLREDPPLEC PVCIDAVQNA VVFFPCGHAT CAECFARITD
PALAVQQGVD GAVEAKCPNC RGKIDPKKVT DYFSFRKLHF PELAGGEDEE LVGIAAVAED
DDSDSDDDSD DEEDDDQDSD LDSFIVPDDY DEEDDAKAST KKSDDSEYKP KSKKSEKSKS
TKSKGKAKKK EKKTLAVLRR EGQRNASSKR KYFKRLEKKW ITSAKIEKAI EILEGIKESG
KGEKTIIFSQ FTSLLDMLEV PINRRGWKYR RYDGSMNPRE RNESVLEFTD KPDCDIMLVS
LKAGNAGLNL VAASQVIIFD PFWNPYIEEQ AIDRAHRLGQ TRPVQVHRIL VEKTVEDRIL
ELQDKKREVI EGALDEHAAS QISRLGVREL KFLFNVQ
//
